Crystallization and preliminary X-ray crystallographic analysis of Escherichia coliglutaredoxin 2 in complex with glutathione and of a cysteine-less variant without glutathione.
Identifieur interne : 000C90 ( Main/Exploration ); précédent : 000C89; suivant : 000C91Crystallization and preliminary X-ray crystallographic analysis of Escherichia coliglutaredoxin 2 in complex with glutathione and of a cysteine-less variant without glutathione.
Auteurs : Ju Sheng [États-Unis] ; Jun Ye ; Barry P. RosenSource :
- Acta crystallographica. Section F, Structural biology and crystallization communications [ 1744-3091 ] ; 2007.
Descripteurs français
- KwdFr :
- MESH :
- composition chimique : Cystéine, Glutathion, Oxidoreductases.
- enzymologie : Escherichia coli.
- Conformation des protéines, Cristallisation, Cristallographie aux rayons X, Glutarédoxines.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Cysteine, Glutathione, Oxidoreductases.
- enzymology : Escherichia coli.
- Crystallization, Crystallography, X-Ray, Glutaredoxins, Protein Conformation.
Abstract
Glutaredoxin 2 (Grx2) from Escherichia coli is larger in size than classical glutaredoxins. It is extremely efficient in the catalysis of reduced glutathione-dependent disulfide reduction. A complex of Grx2 with reduced glutathione (GSH) has been crystallized. Data were collected to 1.60 A. The crystals belong to space group P3(2)21, with one Grx2-GSH complex in the asymmetric unit. The unit-cell parameters are a = b = 50.10, c = 152.47 A. A Grx2 mutant, C9S/C12S, which cannot form a disulfide bond with GSH was also crystallized. The crystals diffracted to 2.40 A and belong to space group P2(1)2(1)2(1), with one molecule in the asymmetric unit. The unit-cell parameters are a = 28.16, b = 78.65, c = 89.16 A.
DOI: 10.1107/S1744309107004204
PubMed: 17401194
PubMed Central: PMC2330212
Affiliations:
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Rosen</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2007">2007</date><idno type="RBID">pubmed:17401194</idno><idno type="pmid">17401194</idno><idno type="doi">10.1107/S1744309107004204</idno><idno type="pmc">PMC2330212</idno><idno type="wicri:Area/Main/Corpus">000C71</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000C71</idno><idno type="wicri:Area/Main/Curation">000C71</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000C71</idno><idno type="wicri:Area/Main/Exploration">000C71</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Crystallization and preliminary X-ray crystallographic analysis of Escherichia coliglutaredoxin 2 in complex with glutathione and of a cysteine-less variant without glutathione.</title><author><name sortKey="Sheng, Ju" sort="Sheng, Ju" uniqKey="Sheng J" first="Ju" last="Sheng">Ju Sheng</name><affiliation wicri:level="2"><nlm:affiliation>Department of Biochemistry and Molecular Biology, Wayne State University, School of Medicine, Detroit, Michigan, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry and Molecular Biology, Wayne State University, School of Medicine, Detroit, Michigan</wicri:regionArea><placeName><region type="state">Michigan</region></placeName></affiliation></author><author><name sortKey="Ye, Jun" sort="Ye, Jun" uniqKey="Ye J" first="Jun" last="Ye">Jun Ye</name></author><author><name sortKey="Rosen, Barry P" sort="Rosen, Barry P" uniqKey="Rosen B" first="Barry P" last="Rosen">Barry P. Rosen</name></author></analytic><series><title level="j">Acta crystallographica. Section F, Structural biology and crystallization communications</title><idno type="eISSN">1744-3091</idno><imprint><date when="2007" type="published">2007</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>Cysteine (chemistry)</term><term>Escherichia coli (enzymology)</term><term>Glutaredoxins (MeSH)</term><term>Glutathione (chemistry)</term><term>Oxidoreductases (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>Cystéine (composition chimique)</term><term>Escherichia coli (enzymologie)</term><term>Glutarédoxines (MeSH)</term><term>Glutathion (composition chimique)</term><term>Oxidoreductases (composition chimique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cysteine</term><term>Glutathione</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Cystéine</term><term>Glutathion</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Crystallization</term><term>Crystallography, X-Ray</term><term>Glutaredoxins</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><term>Glutarédoxines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutaredoxin 2 (Grx2) from Escherichia coli is larger in size than classical glutaredoxins. It is extremely efficient in the catalysis of reduced glutathione-dependent disulfide reduction. A complex of Grx2 with reduced glutathione (GSH) has been crystallized. Data were collected to 1.60 A. The crystals belong to space group P3(2)21, with one Grx2-GSH complex in the asymmetric unit. The unit-cell parameters are a = b = 50.10, c = 152.47 A. A Grx2 mutant, C9S/C12S, which cannot form a disulfide bond with GSH was also crystallized. The crystals diffracted to 2.40 A and belong to space group P2(1)2(1)2(1), with one molecule in the asymmetric unit. The unit-cell parameters are a = 28.16, b = 78.65, c = 89.16 A.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17401194</PMID><DateCompleted><Year>2007</Year><Month>05</Month><Day>31</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1744-3091</ISSN><JournalIssue CitedMedium="Internet"><Volume>63</Volume><Issue>Pt 4</Issue><PubDate><Year>2007</Year><Month>Apr</Month><Day>01</Day></PubDate></JournalIssue><Title>Acta crystallographica. Section F, Structural biology and crystallization communications</Title><ISOAbbreviation>Acta Crystallogr Sect F Struct Biol Cryst Commun</ISOAbbreviation></Journal><ArticleTitle>Crystallization and preliminary X-ray crystallographic analysis of Escherichia coliglutaredoxin 2 in complex with glutathione and of a cysteine-less variant without glutathione.</ArticleTitle><Pagination><MedlinePgn>280-2</MedlinePgn></Pagination><Abstract><AbstractText>Glutaredoxin 2 (Grx2) from Escherichia coli is larger in size than classical glutaredoxins. It is extremely efficient in the catalysis of reduced glutathione-dependent disulfide reduction. A complex of Grx2 with reduced glutathione (GSH) has been crystallized. Data were collected to 1.60 A. The crystals belong to space group P3(2)21, with one Grx2-GSH complex in the asymmetric unit. The unit-cell parameters are a = b = 50.10, c = 152.47 A. A Grx2 mutant, C9S/C12S, which cannot form a disulfide bond with GSH was also crystallized. The crystals diffracted to 2.40 A and belong to space group P2(1)2(1)2(1), with one molecule in the asymmetric unit. The unit-cell parameters are a = 28.16, b = 78.65, c = 89.16 A.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sheng</LastName><ForeName>Ju</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, Wayne State University, School of Medicine, Detroit, Michigan, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ye</LastName><ForeName>Jun</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Rosen</LastName><ForeName>Barry P</ForeName><Initials>BP</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 GM055425</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2007</Year><Month>03</Month><Day>12</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Acta Crystallogr Sect F Struct Biol Cryst Commun</MedlineTA><NlmUniqueID>101226117</NlmUniqueID><ISSNLinking>1744-3091</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical><Chemical><RegistryNumber>K848JZ4886</RegistryNumber><NameOfSubstance UI="D003545">Cysteine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D003460" MajorTopicYN="N">Crystallization</DescriptorName></MeshHeading><MeshHeading><DescriptorName 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IdType="pubmed">11031118</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Michigan</li></region></list><tree><noCountry><name sortKey="Rosen, Barry P" sort="Rosen, Barry P" uniqKey="Rosen B" first="Barry P" last="Rosen">Barry P. Rosen</name><name sortKey="Ye, Jun" sort="Ye, Jun" uniqKey="Ye J" first="Jun" last="Ye">Jun Ye</name></noCountry><country name="États-Unis"><region name="Michigan"><name sortKey="Sheng, Ju" sort="Sheng, Ju" uniqKey="Sheng J" first="Ju" last="Sheng">Ju Sheng</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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