H, C and 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 metabolism of these bacteria. We report the full H, C and N resonance assignments of the reduced and the oxidized form of desulfothioredoxin (DTrx). 2D and 3D heteronuclear NMR experiments were performed using uniformly N-, C-labelled DTrx. More than 98% backbone and 96% side-chain H, C and N resonance assignments were obtained. (BMRB deposits with accession number 16712 and 16713). [ABSTRACT FROM AUTHOR]