摘要：YkuV (148 amino acids) fromBacillus subtilisis identified as a new thioredoxin-like protein based onsequence homology. Thioredoxin is a ubiquitous protein, which serves as a general protein disulfide oxi-doreductase (Holmgren, 1985). Bioinformatics analysis of YkuV shows that protein ResA shares the mosthomologous in PDB database (19%identity), which is the soluble domain of a membrane-anchored pro-tein. (Craw et al., 2004). We report the nearly complete1H,13C and15N resonance assignments of YkuV.2D and 3D heteronuclear NMR experiments were performed with uniformly15N-,13C-labelled YkuV.More than 97%backbone and 90%side-chain1H,13Cand15N resonance assignments are obtained with theexception of residues H42, S131, M133 and K134. BMRB deposits with accession number 6603.
