High-resolution crystal structure of the reduced Grx1 from Saccharomyces cerevisiae.
Identifieur interne : 000157 ( Main/Exploration ); précédent : 000156; suivant : 000158High-resolution crystal structure of the reduced Grx1 from Saccharomyces cerevisiae.
Auteurs : Shadi Maghool [Australie] ; Sharon La Fontaine [Australie] ; Megan J. Maher [Australie]Source :
- Acta crystallographica. Section F, Structural biology communications [ 2053-230X ] ; 2019.
Descripteurs français
- KwdFr :
- Clonage moléculaire (MeSH), Cristallographie aux rayons X (MeSH), Cystéine (composition chimique), Domaine catalytique (MeSH), Escherichia coli (génétique), Escherichia coli (métabolisme), Expression des gènes (MeSH), Glutarédoxines (composition chimique), Glutarédoxines (génétique), Glutarédoxines (métabolisme), Glutathion (composition chimique), Glutathion (métabolisme), Liaison aux protéines (MeSH), Modèles moléculaires (MeSH), Motifs et domaines d'intéraction protéique (MeSH), Multimérisation de protéines (MeSH), Oxydoréduction (MeSH), Protéines de Saccharomyces cerevisiae (composition chimique), Protéines de Saccharomyces cerevisiae (génétique), Protéines de Saccharomyces cerevisiae (métabolisme), Protéines recombinantes (composition chimique), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), Relation structure-activité (MeSH), Saccharomyces cerevisiae (composition chimique), Saccharomyces cerevisiae (enzymologie), Similitude structurale de protéines (MeSH), Spécificité du substrat (MeSH), Structure en brin bêta (MeSH), Structure en hélice alpha (MeSH), Séquence d'acides aminés (MeSH), Vecteurs génétiques (composition chimique), Vecteurs génétiques (métabolisme).
- MESH :
- composition chimique : Cystéine, Glutarédoxines, Glutathion, Protéines de Saccharomyces cerevisiae, Protéines recombinantes, Saccharomyces cerevisiae, Vecteurs génétiques.
- enzymologie : Saccharomyces cerevisiae.
- génétique : Escherichia coli, Glutarédoxines, Protéines de Saccharomyces cerevisiae, Protéines recombinantes.
- métabolisme : Escherichia coli, Glutarédoxines, Glutathion, Protéines de Saccharomyces cerevisiae, Protéines recombinantes, Vecteurs génétiques.
- Clonage moléculaire, Cristallographie aux rayons X, Domaine catalytique, Expression des gènes, Liaison aux protéines, Modèles moléculaires, Motifs et domaines d'intéraction protéique, Multimérisation de protéines, Oxydoréduction, Relation structure-activité, Similitude structurale de protéines, Spécificité du substrat, Structure en brin bêta, Structure en hélice alpha, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Catalytic Domain (MeSH), Cloning, Molecular (MeSH), Crystallography, X-Ray (MeSH), Cysteine (chemistry), Escherichia coli (genetics), Escherichia coli (metabolism), Gene Expression (MeSH), Genetic Vectors (chemistry), Genetic Vectors (metabolism), Glutaredoxins (chemistry), Glutaredoxins (genetics), Glutaredoxins (metabolism), Glutathione (chemistry), Glutathione (metabolism), Models, Molecular (MeSH), Oxidation-Reduction (MeSH), Protein Binding (MeSH), Protein Conformation, alpha-Helical (MeSH), Protein Conformation, beta-Strand (MeSH), Protein Interaction Domains and Motifs (MeSH), Protein Multimerization (MeSH), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Saccharomyces cerevisiae (chemistry), Saccharomyces cerevisiae (enzymology), Saccharomyces cerevisiae Proteins (chemistry), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Structural Homology, Protein (MeSH), Structure-Activity Relationship (MeSH), Substrate Specificity (MeSH).
- MESH :
- chemical , chemistry : Cysteine, Glutaredoxins, Glutathione, Recombinant Proteins, Saccharomyces cerevisiae Proteins.
- chemistry : Genetic Vectors, Saccharomyces cerevisiae.
- enzymology : Saccharomyces cerevisiae.
- genetics : Escherichia coli, Glutaredoxins, Recombinant Proteins, Saccharomyces cerevisiae Proteins.
- metabolism : Escherichia coli, Genetic Vectors, Glutaredoxins, Glutathione, Recombinant Proteins, Saccharomyces cerevisiae Proteins.
- Amino Acid Sequence, Catalytic Domain, Cloning, Molecular, Crystallography, X-Ray, Gene Expression, Models, Molecular, Oxidation-Reduction, Protein Binding, Protein Conformation, alpha-Helical, Protein Conformation, beta-Strand, Protein Interaction Domains and Motifs, Protein Multimerization, Structural Homology, Protein, Structure-Activity Relationship, Substrate Specificity.
Abstract
Grx1, a cytosolic thiol-disulfide oxidoreductase, actively maintains cellular redox homeostasis using glutathione substrates (reduced, GSH, and oxidized, GSSG). Here, the crystallization of reduced Grx1 from the yeast Saccharomyces cerevisiae (yGrx1) in space group P212121 and its structure solution and refinement to 1.22 Å resolution are reported. To study the structure-function relationship of yeast Grx1, the crystal structure of reduced yGrx1 was compared with the existing structures of the oxidized and glutathionylated forms. These comparisons revealed structural differences in the conformations of residues neighbouring the Cys27-Cys30 active site which accompany alterations in the redox status of the protein.
DOI: 10.1107/S2053230X19003327
PubMed: 31045569
PubMed Central: PMC6497100
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Maher</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, Victoria, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Department of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, Victoria</wicri:regionArea><wicri:noRegion>Victoria</wicri:noRegion></affiliation></author></analytic><series><title level="j">Acta crystallographica. 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(MeSH)</term><term>Protein Conformation, beta-Strand (MeSH)</term><term>Protein Interaction Domains and Motifs (MeSH)</term><term>Protein Multimerization (MeSH)</term><term>Recombinant Proteins (chemistry)</term><term>Recombinant Proteins (genetics)</term><term>Recombinant Proteins (metabolism)</term><term>Saccharomyces cerevisiae (chemistry)</term><term>Saccharomyces cerevisiae (enzymology)</term><term>Saccharomyces cerevisiae Proteins (chemistry)</term><term>Saccharomyces cerevisiae Proteins (genetics)</term><term>Saccharomyces cerevisiae Proteins (metabolism)</term><term>Structural Homology, Protein (MeSH)</term><term>Structure-Activity Relationship (MeSH)</term><term>Substrate Specificity (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Clonage moléculaire (MeSH)</term><term>Cristallographie aux rayons X (MeSH)</term><term>Cystéine (composition chimique)</term><term>Domaine catalytique (MeSH)</term><term>Escherichia coli (génétique)</term><term>Escherichia coli (métabolisme)</term><term>Expression des gènes (MeSH)</term><term>Glutarédoxines (composition chimique)</term><term>Glutarédoxines (génétique)</term><term>Glutarédoxines (métabolisme)</term><term>Glutathion (composition chimique)</term><term>Glutathion (métabolisme)</term><term>Liaison aux protéines (MeSH)</term><term>Modèles moléculaires (MeSH)</term><term>Motifs et domaines d'intéraction protéique (MeSH)</term><term>Multimérisation de protéines (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Protéines de Saccharomyces cerevisiae (composition chimique)</term><term>Protéines de Saccharomyces cerevisiae (génétique)</term><term>Protéines de Saccharomyces cerevisiae (métabolisme)</term><term>Protéines recombinantes (composition chimique)</term><term>Protéines recombinantes (génétique)</term><term>Protéines recombinantes (métabolisme)</term><term>Relation structure-activité (MeSH)</term><term>Saccharomyces cerevisiae (composition chimique)</term><term>Saccharomyces cerevisiae (enzymologie)</term><term>Similitude structurale de protéines (MeSH)</term><term>Spécificité du substrat (MeSH)</term><term>Structure en brin bêta (MeSH)</term><term>Structure en hélice alpha (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Vecteurs génétiques (composition chimique)</term><term>Vecteurs génétiques (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cysteine</term><term>Glutaredoxins</term><term>Glutathione</term><term>Recombinant Proteins</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Genetic Vectors</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Cystéine</term><term>Glutarédoxines</term><term>Glutathion</term><term>Protéines de Saccharomyces cerevisiae</term><term>Protéines recombinantes</term><term>Saccharomyces cerevisiae</term><term>Vecteurs génétiques</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Escherichia coli</term><term>Glutaredoxins</term><term>Recombinant Proteins</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Escherichia coli</term><term>Glutarédoxines</term><term>Protéines de Saccharomyces cerevisiae</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Escherichia coli</term><term>Genetic Vectors</term><term>Glutaredoxins</term><term>Glutathione</term><term>Recombinant Proteins</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Escherichia coli</term><term>Glutarédoxines</term><term>Glutathion</term><term>Protéines de Saccharomyces cerevisiae</term><term>Protéines recombinantes</term><term>Vecteurs génétiques</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Catalytic Domain</term><term>Cloning, Molecular</term><term>Crystallography, X-Ray</term><term>Gene Expression</term><term>Models, Molecular</term><term>Oxidation-Reduction</term><term>Protein Binding</term><term>Protein Conformation, alpha-Helical</term><term>Protein Conformation, beta-Strand</term><term>Protein Interaction Domains and Motifs</term><term>Protein Multimerization</term><term>Structural Homology, Protein</term><term>Structure-Activity Relationship</term><term>Substrate Specificity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Clonage moléculaire</term><term>Cristallographie aux rayons X</term><term>Domaine catalytique</term><term>Expression des gènes</term><term>Liaison aux protéines</term><term>Modèles moléculaires</term><term>Motifs et domaines d'intéraction protéique</term><term>Multimérisation de protéines</term><term>Oxydoréduction</term><term>Relation structure-activité</term><term>Similitude structurale de protéines</term><term>Spécificité du substrat</term><term>Structure en brin bêta</term><term>Structure en hélice alpha</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Grx1, a cytosolic thiol-disulfide oxidoreductase, actively maintains cellular redox homeostasis using glutathione substrates (reduced, GSH, and oxidized, GSSG). Here, the crystallization of reduced Grx1 from the yeast Saccharomyces cerevisiae (yGrx1) in space group P2<sub>1</sub>2<sub>1</sub>2<sub>1</sub> and its structure solution and refinement to 1.22 Å resolution are reported. To study the structure-function relationship of yeast Grx1, the crystal structure of reduced yGrx1 was compared with the existing structures of the oxidized and glutathionylated forms. These comparisons revealed structural differences in the conformations of residues neighbouring the Cys27-Cys30 active site which accompany alterations in the redox status of the protein.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">31045569</PMID><DateCompleted><Year>2019</Year><Month>08</Month><Day>26</Day></DateCompleted><DateRevised><Year>2020</Year><Month>10</Month><Day>28</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">2053-230X</ISSN><JournalIssue CitedMedium="Internet"><Volume>75</Volume><Issue>Pt 5</Issue><PubDate><Year>2019</Year><Month>May</Month><Day>01</Day></PubDate></JournalIssue><Title>Acta crystallographica. Section F, Structural biology communications</Title><ISOAbbreviation>Acta Crystallogr F Struct Biol Commun</ISOAbbreviation></Journal><ArticleTitle>High-resolution crystal structure of the reduced Grx1 from Saccharomyces cerevisiae.</ArticleTitle><Pagination><MedlinePgn>392-396</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1107/S2053230X19003327</ELocationID><Abstract><AbstractText>Grx1, a cytosolic thiol-disulfide oxidoreductase, actively maintains cellular redox homeostasis using glutathione substrates (reduced, GSH, and oxidized, GSSG). Here, the crystallization of reduced Grx1 from the yeast Saccharomyces cerevisiae (yGrx1) in space group P2<sub>1</sub>2<sub>1</sub>2<sub>1</sub> and its structure solution and refinement to 1.22 Å resolution are reported. To study the structure-function relationship of yeast Grx1, the crystal structure of reduced yGrx1 was compared with the existing structures of the oxidized and glutathionylated forms. These comparisons revealed structural differences in the conformations of residues neighbouring the Cys27-Cys30 active site which accompany alterations in the redox status of the protein.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Maghool</LastName><ForeName>Shadi</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, Victoria, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>La Fontaine</LastName><ForeName>Sharon</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>School of Life and Environmental Sciences, Deakin University, Melbourne, Victoria, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Maher</LastName><ForeName>Megan J</ForeName><Initials>MJ</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, Victoria, Australia.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>DP140102746</GrantID><Agency>Australian Research Council</Agency><Country></Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2019</Year><Month>04</Month><Day>26</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Acta Crystallogr F Struct Biol Commun</MedlineTA><NlmUniqueID>101620319</NlmUniqueID><ISSNLinking>2053-230X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C530831">Grx1 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical><Chemical><RegistryNumber>K848JZ4886</RegistryNumber><NameOfSubstance UI="D003545">Cysteine</NameOfSubstance></Chemical></ChemicalList><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020134" MajorTopicYN="N">Catalytic Domain</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003545" MajorTopicYN="N">Cysteine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015870" MajorTopicYN="N">Gene Expression</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005822" MajorTopicYN="N">Genetic Vectors</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000072756" MajorTopicYN="N">Protein Conformation, alpha-Helical</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000072757" MajorTopicYN="N">Protein Conformation, beta-Strand</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054730" MajorTopicYN="N">Protein Interaction Domains and Motifs</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055503" MajorTopicYN="N">Protein Multimerization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029701" MajorTopicYN="N">Saccharomyces cerevisiae Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D040681" MajorTopicYN="N">Structural Homology, Protein</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013329" MajorTopicYN="N">Structure-Activity Relationship</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Grx1</Keyword><Keyword MajorTopicYN="N">Saccharomyces cerevisiae</Keyword><Keyword MajorTopicYN="N">glutaredoxin</Keyword><Keyword MajorTopicYN="N">reduced form</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2018</Year><Month>11</Month><Day>18</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2019</Year><Month>03</Month><Day>07</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2019</Year><Month>5</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2019</Year><Month>5</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2019</Year><Month>8</Month><Day>27</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">31045569</ArticleId><ArticleId IdType="pii">S2053230X19003327</ArticleId><ArticleId IdType="doi">10.1107/S2053230X19003327</ArticleId><ArticleId IdType="pmc">PMC6497100</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Structure. 1995 Mar 15;3(3):245-50</Citation><ArticleIdList><ArticleId IdType="pubmed">7788290</ArticleId></ArticleIdList></Reference><Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2011 Apr;67(Pt 4):355-67</Citation><ArticleIdList><ArticleId 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