Fast conformational exchange between the sulfur-free and persulfide-bound rhodanese domain of E. coli YgaP.
Biochem Biophys Res Commun
; 452(3): 817-21, 2014 Sep 26.
Article
em En
| MEDLINE
| ID: mdl-25204500
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.
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Texto completo:
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Base de dados:
MEDLINE
Assunto principal:
Sulfetos
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Enxofre
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Tiossulfato Sulfurtransferase
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Proteínas de Escherichia coli
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Escherichia coli
Idioma:
En
Revista:
Biochem Biophys Res Commun
Ano de publicação:
2014
Tipo de documento:
Article