Fast conformational exchange between the sulfur-free and persulfide-bound rhodanese domain of E. coli YgaP.

Rhodanese domains are abundant structural modules that catalyze the transfer of a sulfur atom from thiolsulfates to cyanide via formation of a covalent persulfide intermediate that is bound to an essential conserved cysteine residue. In this study, the three-dimensional structure of the rhodanese domain of YgaP from Escherichia coli was determined using solution NMR. A typical rhodanese domain fold was observed, as expected from the high homology with the catalytic domain of other sulfur transferases. The initial sulfur-transfer step and formation of the rhodanese persulfide intermediate were monitored by addition of sodium thiosulfate using two-dimensional (1)H-(15)N correlation spectroscopy. Discrete sharp signals were observed upon substrate addition, indicting fast exchange between sulfur-free and persulfide-intermediate forms. Residues exhibiting pronounced chemical shift changes were mapped to the structure, and included both substrate binding and surrounding residues. Copyright © 2014 Elsevier Inc. All rights reserved.

Citation

Wei Wang, Peng Zhou, Yao He, Lu Yu, Ying Xiong, Changlin Tian, Fangming Wu. Fast conformational exchange between the sulfur-free and persulfide-bound rhodanese domain of E. coli YgaP. Biochemical and biophysical research communications. 2014 Sep 26;452(3):817-21

Mesh Tags

Substances

PMID: 25204500

search → result