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

Edwige B Garcin , Olivier Bornet (1) , Laetitia Pieulle , Françoise Guerlesquin (1) , Corinne Sebban-Kreuzer

1 IMR - Interactions et Modulateurs de Réponses

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).

Domaines: Biochimie, Biologie Moléculaire

Edwige B Garcin, Olivier Bornet, Laetitia Pieulle, Françoise Guerlesquin, Corinne Sebban-Kreuzer. (1)H, (13)C and (15)N backbone and side-chain chemical shift assignments for oxidized and reduced desulfothioredoxin.. Biomolecular NMR Assignments, 2010, epub ahead of print. ⟨10.1007/s12104-010-9226-9⟩. ⟨hal-00473694⟩