Structure of Escherichia coli Grx2 in complex with glutathione: a dual-function hybrid of glutaredoxin and glutathione S-transferase.
Identifieur interne : 000599 ( Main/Exploration ); précédent : 000598; suivant : 000600Structure of Escherichia coli Grx2 in complex with glutathione: a dual-function hybrid of glutaredoxin and glutathione S-transferase.
Auteurs : Jun Ye [République populaire de Chine] ; S Venkadesh Nadar [États-Unis] ; Jiaojiao Li [États-Unis] ; Barry P. Rosen [États-Unis]Source :
- Acta crystallographica. Section D, Biological crystallography [ 1399-0047 ] ; 2014.
Descripteurs français
- KwdFr :
- MESH :
- composition chimique : Escherichia coli, Glutarédoxines, Glutathion.
- Conformation des protéines, Cristallisation, Cristallographie aux rayons X.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Glutaredoxins, Glutathione.
- chemistry : Escherichia coli.
- Crystallization, Crystallography, X-Ray, Protein Conformation.
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.
DOI: 10.1107/S1399004714009250
PubMed: 25004967
PubMed Central: PMC4984262
Affiliations:
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Rosen</name><affiliation wicri:level="2"><nlm:affiliation>Department of Cellular Biology and Pharmacology, Florida International University, Herbert Wertheim College of Medicine, Miami, FL 33199, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Cellular Biology and Pharmacology, Florida International University, Herbert Wertheim College of Medicine, Miami, FL 33199</wicri:regionArea><placeName><region type="state">Floride</region></placeName></affiliation></author></analytic><series><title level="j">Acta crystallographica. Section D, Biological crystallography</title><idno type="eISSN">1399-0047</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Crystallization (MeSH)</term><term>Crystallography, X-Ray (MeSH)</term><term>Escherichia coli (chemistry)</term><term>Glutaredoxins (chemistry)</term><term>Glutathione (chemistry)</term><term>Protein Conformation (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Conformation des protéines (MeSH)</term><term>Cristallisation (MeSH)</term><term>Cristallographie aux rayons X (MeSH)</term><term>Escherichia coli (composition chimique)</term><term>Glutarédoxines (composition chimique)</term><term>Glutathion (composition chimique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glutaredoxins</term><term>Glutathione</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Escherichia coli</term><term>Glutarédoxines</term><term>Glutathion</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Crystallization</term><term>Crystallography, X-Ray</term><term>Protein Conformation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Conformation des protéines</term><term>Cristallisation</term><term>Cristallographie aux rayons X</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">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. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25004967</PMID><DateCompleted><Year>2015</Year><Month>03</Month><Day>30</Day></DateCompleted><DateRevised><Year>2019</Year><Month>01</Month><Day>12</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1399-0047</ISSN><JournalIssue CitedMedium="Internet"><Volume>70</Volume><Issue>Pt 7</Issue><PubDate><Year>2014</Year><Month>Jul</Month></PubDate></JournalIssue><Title>Acta crystallographica. Section D, Biological crystallography</Title><ISOAbbreviation>Acta Crystallogr D Biol Crystallogr</ISOAbbreviation></Journal><ArticleTitle>Structure of Escherichia coli Grx2 in complex with glutathione: a dual-function hybrid of glutaredoxin and glutathione S-transferase.</ArticleTitle><Pagination><MedlinePgn>1907-13</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1107/S1399004714009250</ELocationID><Abstract><AbstractText>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. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ye</LastName><ForeName>Jun</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Key Laboratory of Urban Environment and Health, Institute of Urban Environment, Chinese Academy of Sciences, Xiamen, People's Republic of China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nadar</LastName><ForeName>S Venkadesh</ForeName><Initials>SV</Initials><AffiliationInfo><Affiliation>Department of Cellular Biology and Pharmacology, Florida International University, Herbert Wertheim College of Medicine, Miami, FL 33199, USA.</Affiliation></AffiliationInfo></Author><Author 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