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

• Published in: Biomolecular NMR assignments Vol. 4; no. 2; pp. 135 - 137
• Main Authors: Garcin, Edwige B., Bornet, Olivier, Pieulle, Laetitia, Guerlesquin, Françoise, Sebban-Kreuzer, Corinne
• Format: Journal Article
• Language: English
• Published: Dordrecht Springer Netherlands 01.10.2010; Springer Nature B.V
• Subjects: Amino acids; Biochemistry; Biological and Medical Physics; Biophysics; Carbon Isotopes; Desulfovibrio vulgaris - chemistry; Hydrogen; Molecular biology; Nitrogen Isotopes; NMR; Nuclear magnetic resonance; Nuclear Magnetic Resonance, Biomolecular; Oxidation; Oxidation-Reduction; Physics; Physics and Astronomy; Polymer Sciences; Thioredoxins - chemistry; Hildenborough; NMR and; Thioredoxin; Desulfothioredoxin; Protein
• ISSN: 1874-2718; 1874-270X; 1874-270X
• DOI: 10.1007/s12104-010-9226-9

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).