1H, 13C and 15N chemical shift assignments of the thioredoxin from the obligate anaerobe Desulfovibrio vulgaris Hildenborough.

Edwige B Garcin , Olivier Bornet (1) , Laetitia Pieulle (1) , Françoise Guerlesquin (2) , Corinne Sebban-Kreuzer (1)

1 IMR - Interactions et Modulateurs de Réponses
2 LISM - Laboratoire d'ingénierie des systèmes macromoléculaires

Thioredoxins are ubiquitous key antioxidant enzymes which play an essential role in cell defense against oxidative stress. They maintain the redox homeostasis owing to the regulation of thiol-disulfide exchange. In the present paper, we report the full resonance assignments of (1)H, (13)C and (15)N atoms for the reduced and oxidized forms of Desulfovibrio vulgaris Hildenborough thioredoxin 1 (Trx1). 2D and 3D heteronuclear NMR experiments were performed using uniformly (15)N-, (13)C-labelled Trx1. Chemical shifts of 97% of the backbone and 90% of the side chain atoms were obtained for the oxidized and reduced form (BMRB deposits with accession number 17299 and 17300, respectively).

Domaines: Biochimie, Biologie Moléculaire

Edwige B Garcin, Olivier Bornet, Laetitia Pieulle, Françoise Guerlesquin, Corinne Sebban-Kreuzer. 1H, 13C and 15N chemical shift assignments of the thioredoxin from the obligate anaerobe Desulfovibrio vulgaris Hildenborough.. Biomol NMR Assign, 2011, 5 (2), pp.177--9. ⟨10.1007/s12104-011-9294-5⟩. ⟨hal-01458276⟩