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

Abstract：

: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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Wang W,Zhou P,He Y,Yu L,Xiong Y,Tian C,Wu F

doi

10.1016/j.bbrc.2014.09.002

subject

Has Abstract

pub_date

2014-09-26 00:00:00

pages

817-21

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(14)01591-5

journal_volume

452

pub_type

杂志文章

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