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Acta Crystallogr D Biol Crystallogr. 2014 Jul;70(Pt 7):1907-13. doi: 10.1107/S1399004714009250. Epub 2014 Jun 29.

Structure of Escherichia coli Grx2 in complex with glutathione: a dual-function hybrid of glutaredoxin and glutathione S-transferase.

Author information

1
Key Laboratory of Urban Environment and Health, Institute of Urban Environment, Chinese Academy of Sciences, Xiamen, People's Republic of China.
2
Department of Cellular Biology and Pharmacology, Florida International University, Herbert Wertheim College of Medicine, Miami, FL 33199, USA.

Abstract

The structure of glutaredoxin 2 (Grx2) from Escherichia coli co-crystallized with glutathione (GSH) was solved at 1.60 Å resolution. The structure of a mutant with the active-site residues Cys9 and Cys12 changed to serine crystallized in the absence of glutathione was solved to 2.4 Å resolution. Grx2 has an N-terminal domain characteristic of glutaredoxins, and the overall structure is congruent with the structure of glutathione S-transferases (GSTs). Purified Grx2 exhibited GST activity. Grx2, which is the physiological electron donor for arsenate reduction by E. coli ArsC, was docked with ArsC. The docked structure could be fitted with GSH bridging the active sites of the two proteins. It is proposed that Grx2 is a novel Grx/GST hybrid that functions in two steps of the ArsC catalytic cycle: as a GST it catalyzes glutathionylation of the ArsC-As(V) intermediate and as a glutaredoxin it catalyzes deglutathionylation of the ArsC-As(III)-SG intermediate.

KEYWORDS:

glutaredoxin 2; glutaredoxin/glutathione S-transferase hybrid; glutathione

PMID:
25004967
PMCID:
PMC4984262
DOI:
10.1107/S1399004714009250
[Indexed for MEDLINE]
Free PMC Article
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