An electron transfer path connects subunits of a mycobacterial respiratory supercomplex
Respiratory complexes are massive, membrane-embedded scaffolds that position redox cofactors so as to permit electron transfer coupled to the movement of protons across a membrane. Gong et al. used cryo–electron microscopy to determine a structure of a stable assembly of mycobacterial complex III–IV...
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| Published in | Science (American Association for the Advancement of Science) Vol. 362; no. 6418 |
|---|---|
| Main Authors | , , , , , , , , , , , , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
The American Association for the Advancement of Science
30.11.2018
|
| Subjects | |
| Online Access | Get full text |
| ISSN | 0036-8075 1095-9203 1095-9203 |
| DOI | 10.1126/science.aat8923 |
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| Abstract | Respiratory complexes are massive, membrane-embedded scaffolds that position redox cofactors so as to permit electron transfer coupled to the movement of protons across a membrane. Gong
et al.
used cryo–electron microscopy to determine a structure of a stable assembly of mycobacterial complex III–IV, in which a complex III dimer is sandwiched between two complex IV monomers. A potential direct electron transfer path stretches from the quinone oxidizing centers in complex III to the oxygen reduction centers in complex IV. A loosely associated superoxide dismutase may play a role in detoxifying superoxide produced from uncoupled oxygen reduction.
Science
, this issue p.
eaat8923
A mycobacterial respiratory supercomplex forgoes soluble electron carriers and associates with superoxide dismutase.
We report a 3.5-angstrom-resolution cryo–electron microscopy structure of a respiratory supercomplex isolated from
Mycobacterium smegmatis.
It comprises a complex III dimer flanked on either side by individual complex IV subunits. Complex III and IV associate so that electrons can be transferred from quinol in complex III to the oxygen reduction center in complex IV by way of a bridging cytochrome subunit. We observed a superoxide dismutase-like subunit at the periplasmic face, which may be responsible for detoxification of superoxide formed by complex III. The structure reveals features of an established drug target and provides a foundation for the development of treatments for human tuberculosis. |
|---|---|
| AbstractList | An electron bridge in place of a ferryRespiratory complexes are massive, membrane-embedded scaffolds that position redox cofactors so as to permit electron transfer coupled to the movement of protons across a membrane. Gong et al. used cryo–electron microscopy to determine a structure of a stable assembly of mycobacterial complex III–IV, in which a complex III dimer is sandwiched between two complex IV monomers. A potential direct electron transfer path stretches from the quinone oxidizing centers in complex III to the oxygen reduction centers in complex IV. A loosely associated superoxide dismutase may play a role in detoxifying superoxide produced from uncoupled oxygen reduction.Science, this issue p. eaat8923INTRODUCTIONCellular respiration is a core feature in the metabolism of many organisms that allows for the generation of a proton gradient across a membrane. During respiration, electrons are transferred from electron donors to oxygen through an electron transport chain. The energy created allows protons to be pumped across a membrane (cellular or mitochondrial). In electron transport chains, quinones and cytochrome c are two of the electron carriers that shuttle electrons to and from large macromolecular structures that are embedded in the membrane. The components that allow respiratory chains to function in the mitochondria are well characterized, but the situation is less clear and more varied in prokaryotic systems. A soluble cytochrome c pathway for electron transfer similar to that in mitochondria is commonly found in Gram-negative bacteria. Gram-positive bacteria such as Mycobacteria are devoid of a soluble cytochrome c but instead possess cytochrome c proteins that are anchored onto the membrane or have a fused cytochrome c domain to mediate electron transfer between two of the major complexes, which are referred to as CIII and CIV.Structures of eukaryotic respiratory supercomplexes have been reported, but cytochrome c is not visible in any of these structures. Thus, a complete pathway for electron flow has not yet been visualized. CIII–CIV supercomplexes have been isolated from Mycobacterium smegmatis, Corynebacterium glutamicum, and Mycobacterium tuberculosis and shown to couple quinol oxidation to oxygen reduction without an external electron shuttle, suggesting that the flow of electrons is internalized in this type of complex. The determination of the structure of this complex reveals a path for electron transfer between the subunits of these supercomplexes.RATIONALEThe structural information provided here is required to understand the molecular details of electron transport in Mycobacteria. We have selected the supercomplex CIII–CIV from M. smegmatis because it is highly similar to the CIII–CIV complex from the human pathogen M. tuberculosis. This complex was amenable to expression and purification and analysis by means of cryo–electron microscopy (cryo-EM).RESULTSWe have determined a cryo-EM structure of a respiratory supercomplex isolated from M. smegmatis. The structure allows the complete visualization of 20 subunits that associate to form the complex. Central to the supercomplex is a CIII dimer that is flanked on either side by individual CIV subunits. Fused c-type cytochrome domains bridge and mediate electron transfer from CIII to CIV. The structure also reveals three previously unidentified associated subunits that contribute to the stability of the supercomplex and the presence of superoxide dismutase (SOD), which may be responsible for the detoxification of superoxide formed by CIII.CONCLUSIONThis study of a respiratory supercomplex in Mycobacteria reveals cofactors positioned at distances that permit electron tunneling, enabling direct intrasupercomplex electron transfer from menaquinol to oxygen without the need for a separate cytochrome c electron shuttle. The presence of a bound SOD to the respiratory supercomplex suggests a mechanism of mycobacterial resistance against exogenous and endogenous oxidative stress in macrophages and host immune responses. The structure of the quinone binding sites provides a framework for rational structure-based M. tuberculosis drug discovery. A binding site can be proposed for the candidate antimycobacterial drug Q203, which acts by inhibiting the activity of this supercomplex.We report a 3.5-angstrom-resolution cryo–electron microscopy structure of a respiratory supercomplex isolated from Mycobacterium smegmatis. It comprises a complex III dimer flanked on either side by individual complex IV subunits. Complex III and IV associate so that electrons can be transferred from quinol in complex III to the oxygen reduction center in complex IV by way of a bridging cytochrome subunit. We observed a superoxide dismutase-like subunit at the periplasmic face, which may be responsible for detoxification of superoxide formed by complex III. The structure reveals features of an established drug target and provides a foundation for the development of treatments for human tuberculosis. We report a 3.5-angstrom-resolution cryo-electron microscopy structure of a respiratory supercomplex isolated from Mycobacterium smegmatis. It comprises a complex III dimer flanked on either side by individual complex IV subunits. Complex III and IV associate so that electrons can be transferred from quinol in complex III to the oxygen reduction center in complex IV by way of a bridging cytochrome subunit. We observed a superoxide dismutase-like subunit at the periplasmic face, which may be responsible for detoxification of superoxide formed by complex III. The structure reveals features of an established drug target and provides a foundation for the development of treatments for human tuberculosis.We report a 3.5-angstrom-resolution cryo-electron microscopy structure of a respiratory supercomplex isolated from Mycobacterium smegmatis. It comprises a complex III dimer flanked on either side by individual complex IV subunits. Complex III and IV associate so that electrons can be transferred from quinol in complex III to the oxygen reduction center in complex IV by way of a bridging cytochrome subunit. We observed a superoxide dismutase-like subunit at the periplasmic face, which may be responsible for detoxification of superoxide formed by complex III. The structure reveals features of an established drug target and provides a foundation for the development of treatments for human tuberculosis. Respiratory complexes are massive, membrane-embedded scaffolds that position redox cofactors so as to permit electron transfer coupled to the movement of protons across a membrane. Gong et al. used cryo–electron microscopy to determine a structure of a stable assembly of mycobacterial complex III–IV, in which a complex III dimer is sandwiched between two complex IV monomers. A potential direct electron transfer path stretches from the quinone oxidizing centers in complex III to the oxygen reduction centers in complex IV. A loosely associated superoxide dismutase may play a role in detoxifying superoxide produced from uncoupled oxygen reduction. Science , this issue p. eaat8923 A mycobacterial respiratory supercomplex forgoes soluble electron carriers and associates with superoxide dismutase. We report a 3.5-angstrom-resolution cryo–electron microscopy structure of a respiratory supercomplex isolated from Mycobacterium smegmatis. It comprises a complex III dimer flanked on either side by individual complex IV subunits. Complex III and IV associate so that electrons can be transferred from quinol in complex III to the oxygen reduction center in complex IV by way of a bridging cytochrome subunit. We observed a superoxide dismutase-like subunit at the periplasmic face, which may be responsible for detoxification of superoxide formed by complex III. The structure reveals features of an established drug target and provides a foundation for the development of treatments for human tuberculosis. We report a 3.5-angstrom-resolution cryo-electron microscopy structure of a respiratory supercomplex isolated from It comprises a complex III dimer flanked on either side by individual complex IV subunits. Complex III and IV associate so that electrons can be transferred from quinol in complex III to the oxygen reduction center in complex IV by way of a bridging cytochrome subunit. We observed a superoxide dismutase-like subunit at the periplasmic face, which may be responsible for detoxification of superoxide formed by complex III. The structure reveals features of an established drug target and provides a foundation for the development of treatments for human tuberculosis. |
| Author | Shui, Guanghou Wong, Luet-Lok Sun, Yuna Gao, Ruogu Lou, Zhiyong Wang, Quan Yang, Xiuna Yen, Hsin-Yung Rao, Zihe Wang, Shuhui Robinson, Carol V. Li, Xuemei Yang, Cheng Jiang, Biao Gong, Hongri Sun, Fei Tang, Yanting Guddat, Luke W. Li, Jun Xu, Ao Ji, Wenxin Li, Jingwen Tian, Changlin Man Lam, Sin Yu, Lu Jia, Minze |
| Author_xml | – sequence: 1 givenname: Hongri orcidid: 0000-0002-2596-7635 surname: Gong fullname: Gong, Hongri organization: State Key Laboratory of Medicinal Chemical Biology and College of Life Science, Nankai University, Tianjin 300353, China – sequence: 2 givenname: Jun orcidid: 0000-0003-3165-3699 surname: Li fullname: Li, Jun organization: Shanghai Institute for Advanced Immunochemical Studies, ShanghaiTech University, Shanghai, 201210, China., CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences (CAS), 320 Yueyang Road, Shanghai 200031, China – sequence: 3 givenname: Ao orcidid: 0000-0002-6153-1644 surname: Xu fullname: Xu, Ao organization: State Key Laboratory of Medicinal Chemical Biology and College of Life Science, Nankai University, Tianjin 300353, China., National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, CAS, Beijing 100101, China – sequence: 4 givenname: Yanting orcidid: 0000-0002-8656-3220 surname: Tang fullname: Tang, Yanting organization: State Key Laboratory of Medicinal Chemical Biology and College of Life Science, Nankai University, Tianjin 300353, China – sequence: 5 givenname: Wenxin orcidid: 0000-0002-3671-1301 surname: Ji fullname: Ji, Wenxin organization: National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, CAS, Beijing 100101, China., University of Chinese Academy of Sciences, Beijing, China – sequence: 6 givenname: Ruogu surname: Gao fullname: Gao, Ruogu organization: National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, CAS, Beijing 100101, China., University of Chinese Academy of Sciences, Beijing, China – sequence: 7 givenname: Shuhui orcidid: 0000-0002-7198-5754 surname: Wang fullname: Wang, Shuhui organization: Shanghai Institute for Advanced Immunochemical Studies, ShanghaiTech University, Shanghai, 201210, China., CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences (CAS), 320 Yueyang Road, Shanghai 200031, China – sequence: 8 givenname: Lu orcidid: 0000-0003-4852-0008 surname: Yu fullname: Yu, Lu organization: High Magnetic Field Laboratory, CAS, Hefei 230031, China – sequence: 9 givenname: Changlin surname: Tian fullname: Tian, Changlin organization: High Magnetic Field Laboratory, CAS, Hefei 230031, China., Hefei National Laboratory of Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei 230027, China – sequence: 10 givenname: Jingwen surname: Li fullname: Li, Jingwen organization: Department of Chemistry, University of Oxford, Physical and Theoretical Chemistry Laboratory, South Parks Rd, Oxford, OX1 3QZ, UK – sequence: 11 givenname: Hsin-Yung surname: Yen fullname: Yen, Hsin-Yung organization: Department of Chemistry, University of Oxford, Physical and Theoretical Chemistry Laboratory, South Parks Rd, Oxford, OX1 3QZ, UK., OMass Technologies, Begbroke Science Park, Woodstock Rd, Yarnton, Kidlington OX5 1PF, UK – sequence: 12 givenname: Sin surname: Man Lam fullname: Man Lam, Sin organization: State Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, CAS, Beijing 100101, China – sequence: 13 givenname: Guanghou surname: Shui fullname: Shui, Guanghou organization: State Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, CAS, Beijing 100101, China – sequence: 14 givenname: Xiuna surname: Yang fullname: Yang, Xiuna organization: Shanghai Institute for Advanced Immunochemical Studies, ShanghaiTech University, Shanghai, 201210, China., CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences (CAS), 320 Yueyang Road, Shanghai 200031, China – sequence: 15 givenname: Yuna surname: Sun fullname: Sun, Yuna organization: National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, CAS, Beijing 100101, China – sequence: 16 givenname: Xuemei surname: Li fullname: Li, Xuemei organization: National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, CAS, Beijing 100101, China – sequence: 17 givenname: Minze surname: Jia fullname: Jia, Minze organization: National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, CAS, Beijing 100101, China – sequence: 18 givenname: Cheng orcidid: 0000-0001-9431-290X surname: Yang fullname: Yang, Cheng organization: State Key Laboratory of Medicinal Chemical Biology and College of Life Science, Nankai University, Tianjin 300353, China – sequence: 19 givenname: Biao surname: Jiang fullname: Jiang, Biao organization: Shanghai Institute for Advanced Immunochemical Studies, ShanghaiTech University, Shanghai, 201210, China – sequence: 20 givenname: Zhiyong surname: Lou fullname: Lou, Zhiyong organization: Laboratory of Structural Biology, Tsinghua University, Beijing 100084, China – sequence: 21 givenname: Carol V. orcidid: 0000-0001-7829-5505 surname: Robinson fullname: Robinson, Carol V. organization: Department of Chemistry, University of Oxford, Physical and Theoretical Chemistry Laboratory, South Parks Rd, Oxford, OX1 3QZ, UK – sequence: 22 givenname: Luet-Lok orcidid: 0000-0003-4875-1092 surname: Wong fullname: Wong, Luet-Lok organization: Department of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, South Parks Road, Oxford OX1 3QR, UK – sequence: 23 givenname: Luke W. surname: Guddat fullname: Guddat, Luke W. organization: School of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, 4072 Queensland, Australia – sequence: 24 givenname: Fei orcidid: 0000-0002-0351-5144 surname: Sun fullname: Sun, Fei organization: National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, CAS, Beijing 100101, China., University of Chinese Academy of Sciences, Beijing, China – sequence: 25 givenname: Quan orcidid: 0000-0001-5148-5210 surname: Wang fullname: Wang, Quan organization: National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, CAS, Beijing 100101, China – sequence: 26 givenname: Zihe orcidid: 0000-0001-9866-2384 surname: Rao fullname: Rao, Zihe organization: State Key Laboratory of Medicinal Chemical Biology and College of Life Science, Nankai University, Tianjin 300353, China., Shanghai Institute for Advanced Immunochemical Studies, ShanghaiTech University, Shanghai, 201210, China., CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences (CAS), 320 Yueyang Road, Shanghai 200031, China., National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, CAS, Beijing 100101, China., Laboratory of Structural Biology, Tsinghua University, Beijing 100084, China |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/30361386$$D View this record in MEDLINE/PubMed |
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| Cites_doi | 10.1038/nmeth.2472 10.1016/j.mib.2014.06.008 10.1016/S0021-9258(18)63504-5 10.1007/s002030100262 10.1093/emboj/19.8.1766 10.1038/355796a0 10.1111/acel.12144 10.1016/j.bbabio.2011.09.020 10.1016/j.ultramic.2013.06.004 10.1016/j.jsb.2015.11.003 10.1038/nmeth.4193 10.1073/pnas.77.1.147 10.1038/cdd.2011.105 10.1038/376660a0 10.1016/j.freeradbiomed.2010.02.020 10.1126/science.280.5370.1723 10.1038/33612 10.1073/pnas.94.20.10547 10.1016/S0076-6879(08)04405-4 10.1007/BF00249037 10.1016/j.jsb.2014.11.010 10.1016/j.cell.2005.05.025 10.1042/bj3590017 10.1093/glycob/cwn102 10.1093/bioinformatics/16.4.404 10.1074/jbc.M404699200 10.1016/j.cmet.2017.03.009 10.1074/jbc.M114.624312 10.7554/eLife.18722 10.1042/bj1910421 10.1002/pmic.200800017 10.1128/JB.188.8.2761-2773.2006 10.1128/genomeA.00092-14 10.1016/j.jmb.2011.11.010 10.1038/nprot.2006.62 10.1038/nmeth.2727 10.1016/j.jsb.2012.09.006 10.1038/s41598-018-20989-8 10.1038/nprot.2015.053 10.1038/nature11871 10.1194/jlr.M044826 10.1038/s41586-018-0061-y 10.1016/S0022-2836(02)00619-8 10.1093/nar/gkw357 10.1038/ncomms5029 10.1111/j.1432-1033.1991.tb15732.x 10.1126/science.1079605 10.1074/jbc.M112.367888 10.1038/nm.3262 10.1016/j.jmb.2003.07.013 10.1016/j.jsb.2006.05.009 10.1107/S0907444909052925 10.1002/jcc.20084 10.1038/nsmb.3460 10.1126/science.277.5322.60 10.1038/nature19774 10.1096/fj.02-0729fje 10.1126/science.281.5373.64 10.1016/B978-0-12-394423-8.00006-8 10.1128/IAI.69.8.4980-4987.2001 10.1038/nature13686 10.1038/srep34098 10.1038/31159 10.1016/S0021-9258(18)89576-X 10.1126/science.1190899 10.1099/mic.0.28723-0 10.1073/pnas.1720702115 10.1016/j.jsb.2005.07.007 10.1038/nmeth.3213 10.1016/S0014-5793(00)01082-6 10.1016/j.bbabio.2016.07.009 10.1099/mic.0.022889-0 10.1042/BST0361022 10.1038/nature19095 10.1016/j.bbabio.2015.11.001 10.1126/science.1123061 10.1007/978-81-322-2035-0_2 10.1016/0076-6879(57)04060-4 10.1016/0005-2728(82)90101-3 10.1016/S0005-2728(00)00205-X 10.1002/emmm.201100185 10.1007/s10863-012-9454-z 10.1016/j.cels.2017.10.017 10.1074/jbc.274.37.26179 10.1074/jbc.M116.744391 10.1074/jbc.273.9.5132 10.1038/191144a0 10.1016/j.bbabio.2009.04.003 10.1021/bi00230a019 10.1126/science.272.5265.1136 10.1107/S0907444910007493 10.15252/embj.201695021 |
| ContentType | Journal Article |
| Copyright | Copyright © 2018 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Copyright © 2018 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works |
| Copyright_xml | – notice: Copyright © 2018 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. – notice: Copyright © 2018 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works |
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| DOI | 10.1126/science.aat8923 |
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| References | e_1_3_2_26_2 e_1_3_2_49_2 e_1_3_2_28_2 e_1_3_2_41_2 e_1_3_2_64_2 e_1_3_2_87_2 e_1_3_2_20_2 e_1_3_2_43_2 e_1_3_2_62_2 e_1_3_2_85_2 Felsenstein J. (e_1_3_2_93_2) 1989; 5 e_1_3_2_22_2 e_1_3_2_45_2 e_1_3_2_68_2 e_1_3_2_24_2 e_1_3_2_47_2 e_1_3_2_66_2 e_1_3_2_89_2 e_1_3_2_60_2 e_1_3_2_83_2 e_1_3_2_81_2 e_1_3_2_9_2 e_1_3_2_16_2 e_1_3_2_37_2 e_1_3_2_7_2 e_1_3_2_18_2 e_1_3_2_39_2 e_1_3_2_54_2 e_1_3_2_75_2 e_1_3_2_10_2 e_1_3_2_31_2 e_1_3_2_52_2 e_1_3_2_73_2 e_1_3_2_5_2 e_1_3_2_12_2 e_1_3_2_33_2 e_1_3_2_58_2 e_1_3_2_79_2 e_1_3_2_3_2 e_1_3_2_14_2 e_1_3_2_35_2 e_1_3_2_56_2 e_1_3_2_77_2 e_1_3_2_92_2 e_1_3_2_94_2 e_1_3_2_50_2 e_1_3_2_71_2 e_1_3_2_90_2 e_1_3_2_27_2 e_1_3_2_48_2 e_1_3_2_29_2 e_1_3_2_40_2 e_1_3_2_65_2 e_1_3_2_86_2 e_1_3_2_21_2 e_1_3_2_42_2 e_1_3_2_63_2 e_1_3_2_84_2 e_1_3_2_23_2 e_1_3_2_44_2 e_1_3_2_69_2 e_1_3_2_25_2 e_1_3_2_46_2 e_1_3_2_67_2 e_1_3_2_88_2 e_1_3_2_61_2 e_1_3_2_82_2 e_1_3_2_80_2 e_1_3_2_15_2 e_1_3_2_38_2 e_1_3_2_8_2 e_1_3_2_17_2 e_1_3_2_59_2 e_1_3_2_6_2 e_1_3_2_19_2 e_1_3_2_30_2 e_1_3_2_53_2 e_1_3_2_76_2 e_1_3_2_32_2 e_1_3_2_51_2 e_1_3_2_74_2 e_1_3_2_11_2 e_1_3_2_34_2 e_1_3_2_57_2 e_1_3_2_95_2 e_1_3_2_4_2 e_1_3_2_13_2 e_1_3_2_36_2 e_1_3_2_55_2 e_1_3_2_78_2 e_1_3_2_2_2 e_1_3_2_91_2 e_1_3_2_72_2 e_1_3_2_70_2 |
| References_xml | – ident: e_1_3_2_74_2 doi: 10.1038/nmeth.2472 – ident: e_1_3_2_53_2 doi: 10.1016/j.mib.2014.06.008 – ident: e_1_3_2_67_2 doi: 10.1016/S0021-9258(18)63504-5 – ident: e_1_3_2_32_2 doi: 10.1007/s002030100262 – ident: e_1_3_2_47_2 doi: 10.1093/emboj/19.8.1766 – ident: e_1_3_2_50_2 doi: 10.1038/355796a0 – ident: e_1_3_2_58_2 doi: 10.1111/acel.12144 – ident: e_1_3_2_38_2 doi: 10.1016/j.bbabio.2011.09.020 – ident: e_1_3_2_77_2 doi: 10.1016/j.ultramic.2013.06.004 – ident: e_1_3_2_76_2 doi: 10.1016/j.jsb.2015.11.003 – ident: e_1_3_2_75_2 doi: 10.1038/nmeth.4193 – ident: e_1_3_2_5_2 doi: 10.1073/pnas.77.1.147 – ident: e_1_3_2_65_2 doi: 10.1038/cdd.2011.105 – ident: e_1_3_2_23_2 doi: 10.1038/376660a0 – ident: e_1_3_2_56_2 doi: 10.1016/j.freeradbiomed.2010.02.020 – ident: e_1_3_2_25_2 doi: 10.1126/science.280.5370.1723 – ident: e_1_3_2_22_2 doi: 10.1038/33612 – ident: e_1_3_2_48_2 doi: 10.1073/pnas.94.20.10547 – ident: e_1_3_2_49_2 doi: 10.1016/S0076-6879(08)04405-4 – ident: e_1_3_2_34_2 doi: 10.1007/BF00249037 – ident: e_1_3_2_70_2 doi: 10.1016/j.jsb.2014.11.010 – ident: e_1_3_2_19_2 doi: 10.1016/j.cell.2005.05.025 – ident: e_1_3_2_36_2 doi: 10.1042/bj3590017 – ident: e_1_3_2_89_2 doi: 10.1093/glycob/cwn102 – ident: e_1_3_2_80_2 doi: 10.1093/bioinformatics/16.4.404 – ident: e_1_3_2_37_2 doi: 10.1074/jbc.M404699200 – volume: 5 start-page: 164 year: 1989 ident: e_1_3_2_93_2 article-title: PHYLIP—Phylogeny Inference Package (Version 3.2) publication-title: Cladistics – ident: e_1_3_2_29_2 doi: 10.1016/j.cmet.2017.03.009 – ident: e_1_3_2_33_2 doi: 10.1074/jbc.M114.624312 – ident: e_1_3_2_73_2 doi: 10.7554/eLife.18722 – ident: e_1_3_2_52_2 doi: 10.1042/bj1910421 – ident: e_1_3_2_61_2 doi: 10.1002/pmic.200800017 – ident: e_1_3_2_35_2 doi: 10.1128/JB.188.8.2761-2773.2006 – ident: e_1_3_2_59_2 doi: 10.1128/genomeA.00092-14 – ident: e_1_3_2_71_2 doi: 10.1016/j.jmb.2011.11.010 – ident: e_1_3_2_60_2 doi: 10.1038/nprot.2006.62 – ident: e_1_3_2_79_2 doi: 10.1038/nmeth.2727 – ident: e_1_3_2_72_2 doi: 10.1016/j.jsb.2012.09.006 – ident: e_1_3_2_43_2 doi: 10.1038/s41598-018-20989-8 – ident: e_1_3_2_81_2 doi: 10.1038/nprot.2015.053 – ident: e_1_3_2_15_2 doi: 10.1038/nature11871 – ident: e_1_3_2_63_2 doi: 10.1194/jlr.M044826 – ident: e_1_3_2_12_2 doi: 10.1038/s41586-018-0061-y – ident: e_1_3_2_39_2 doi: 10.1016/S0022-2836(02)00619-8 – ident: e_1_3_2_92_2 doi: 10.1093/nar/gkw357 – ident: e_1_3_2_41_2 doi: 10.1038/ncomms5029 – ident: e_1_3_2_7_2 doi: 10.1111/j.1432-1033.1991.tb15732.x – ident: e_1_3_2_18_2 doi: 10.1126/science.1079605 – ident: e_1_3_2_27_2 doi: 10.1074/jbc.M112.367888 – ident: e_1_3_2_42_2 doi: 10.1038/nm.3262 – ident: e_1_3_2_78_2 doi: 10.1016/j.jmb.2003.07.013 – ident: e_1_3_2_69_2 doi: 10.1016/j.jsb.2006.05.009 – ident: e_1_3_2_83_2 doi: 10.1107/S0907444909052925 – ident: e_1_3_2_85_2 doi: 10.1002/jcc.20084 – ident: e_1_3_2_28_2 doi: 10.1038/nsmb.3460 – ident: e_1_3_2_20_2 doi: 10.1126/science.277.5322.60 – ident: e_1_3_2_26_2 doi: 10.1038/nature19774 – ident: e_1_3_2_54_2 doi: 10.1096/fj.02-0729fje – ident: e_1_3_2_21_2 doi: 10.1126/science.281.5373.64 – ident: e_1_3_2_40_2 doi: 10.1016/B978-0-12-394423-8.00006-8 – ident: e_1_3_2_57_2 doi: 10.1128/IAI.69.8.4980-4987.2001 – ident: e_1_3_2_16_2 doi: 10.1038/nature13686 – ident: e_1_3_2_66_2 doi: 10.1038/srep34098 – ident: e_1_3_2_9_2 doi: 10.1038/31159 – ident: e_1_3_2_4_2 doi: 10.1016/S0021-9258(18)89576-X – ident: e_1_3_2_44_2 doi: 10.1126/science.1190899 – ident: e_1_3_2_10_2 doi: 10.1099/mic.0.28723-0 – ident: e_1_3_2_31_2 doi: 10.1073/pnas.1720702115 – ident: e_1_3_2_68_2 doi: 10.1016/j.jsb.2005.07.007 – ident: e_1_3_2_84_2 doi: 10.1038/nmeth.3213 – ident: e_1_3_2_55_2 doi: 10.1016/S0014-5793(00)01082-6 – ident: e_1_3_2_11_2 doi: 10.1016/j.bbabio.2016.07.009 – ident: e_1_3_2_95_2 doi: 10.1099/mic.0.022889-0 – ident: e_1_3_2_14_2 doi: 10.1042/BST0361022 – ident: e_1_3_2_17_2 doi: 10.1038/nature19095 – ident: e_1_3_2_3_2 doi: 10.1016/j.bbabio.2015.11.001 – ident: e_1_3_2_94_2 doi: 10.1126/science.1123061 – ident: e_1_3_2_51_2 doi: 10.1007/978-81-322-2035-0_2 – ident: e_1_3_2_86_2 – ident: e_1_3_2_88_2 doi: 10.1016/0076-6879(57)04060-4 – ident: e_1_3_2_87_2 doi: 10.1016/0005-2728(82)90101-3 – ident: e_1_3_2_8_2 doi: 10.1016/S0005-2728(00)00205-X – ident: e_1_3_2_64_2 doi: 10.1002/emmm.201100185 – ident: e_1_3_2_62_2 doi: 10.1007/s10863-012-9454-z – ident: e_1_3_2_30_2 doi: 10.1016/j.cels.2017.10.017 – ident: e_1_3_2_6_2 doi: 10.1074/jbc.274.37.26179 – ident: e_1_3_2_90_2 doi: 10.1074/jbc.M116.744391 – ident: e_1_3_2_45_2 doi: 10.1074/jbc.273.9.5132 – ident: e_1_3_2_2_2 doi: 10.1038/191144a0 – ident: e_1_3_2_91_2 doi: 10.1016/j.bbabio.2009.04.003 – ident: e_1_3_2_13_2 doi: 10.1021/bi00230a019 – ident: e_1_3_2_24_2 doi: 10.1126/science.272.5265.1136 – ident: e_1_3_2_82_2 doi: 10.1107/S0907444910007493 – ident: e_1_3_2_46_2 doi: 10.15252/embj.201695021 |
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| Snippet | Respiratory complexes are massive, membrane-embedded scaffolds that position redox cofactors so as to permit electron transfer coupled to the movement of... We report a 3.5-angstrom-resolution cryo-electron microscopy structure of a respiratory supercomplex isolated from It comprises a complex III dimer flanked on... An electron bridge in place of a ferryRespiratory complexes are massive, membrane-embedded scaffolds that position redox cofactors so as to permit electron... We report a 3.5-angstrom-resolution cryo-electron microscopy structure of a respiratory supercomplex isolated from Mycobacterium smegmatis. It comprises a... |
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| Title | An electron transfer path connects subunits of a mycobacterial respiratory supercomplex |
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