(1)H, (13)C and (15)N backbone and side-chain chemical shift assignments for oxidized and reduced desulfothioredoxin

Based on sequence homology, desulfothioredoxin (DTrx) from Desulfovibrio vulgaris Hildenborough has been identified as a new member of the thioredoxin superfamily. Desulfothioredoxin (104 amino acids) contains a particular active site consensus sequence, CPHC probably correlated to the anaerobic met...

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Published inBiomolecular NMR assignments
Main Authors Garcin, Edwige B, Bornet, Olivier, Pieulle, Laetitia, Guerlesquin, Françoise, Sebban-Kreuzer, Corinne
Format Journal Article
LanguageEnglish
Published Springer 01.10.2010
Subjects
Biochemistry, Molecular Biology
Life Sciences
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ISSN1874-2718
1874-270X
DOI10.1007/s12104-010-9226-9

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Summary:Based on sequence homology, desulfothioredoxin (DTrx) from Desulfovibrio vulgaris Hildenborough has been identified as a new member of the thioredoxin superfamily. Desulfothioredoxin (104 amino acids) contains a particular active site consensus sequence, CPHC probably correlated to the anaerobic metabolism of these bacteria. We report the full (1)H, (13)C and (15)N resonance assignments of the reduced and the oxidized form of desulfothioredoxin (DTrx). 2D and 3D heteronuclear NMR experiments were performed using uniformly (15)N-, (13)C-labelled DTrx. More than 98% backbone and 96% side-chain (1)H, (13)C and (15)N resonance assignments were obtained. (BMRB deposits with accession number 16712 and 16713).
ISSN:1874-2718
1874-270X
DOI:10.1007/s12104-010-9226-9