GlutaredoxinV1, Main, Exploration, bibRecord, 000469

Crystal structure of yeast monothiol glutaredoxin Grx6 in complex with a glutathione-coordinated [2Fe-2S] cluster.

Identifieur interne : 000469 ( Main/Exploration ); précédent : 000468; suivant : 000470

Crystal structure of yeast monothiol glutaredoxin Grx6 in complex with a glutathione-coordinated [2Fe-2S] cluster.

Auteurs : Mohnad Abdalla [République populaire de Chine] ; Ya Nan Dai [République populaire de Chine] ; Chang Biao Chi [République populaire de Chine] ; Wang Cheng [République populaire de Chine] ; Dong Dong Cao [République populaire de Chine] ; Kang Zhou [République populaire de Chine] ; Wafa Ali [République populaire de Chine] ; Yuxing Chen [République populaire de Chine] ; Cong Zhao Zhou [République populaire de Chine]

Source :

Acta crystallographica. Section F, Structural biology communications [ 2053-230X ] ; 2016.

RBID : pubmed:27710937

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Catalytic Domain (MeSH), Cloning, Molecular (MeSH), Coordination Complexes (chemistry), Coordination Complexes (metabolism), Crystallography, X-Ray (MeSH), Escherichia coli (genetics), Escherichia coli (metabolism), Gene Expression (MeSH), Glutaredoxins (chemistry), Glutaredoxins (genetics), Glutaredoxins (metabolism), Glutathione (chemistry), Glutathione (metabolism), Iron (chemistry), Iron (metabolism), Models, Molecular (MeSH), Plasmids (chemistry), Plasmids (metabolism), 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), Sequence Alignment (MeSH), Sequence Homology, Amino Acid (MeSH), Sulfur (chemistry), Sulfur (metabolism).
MESH :
- chemical , chemistry : Coordination Complexes, Glutaredoxins, Glutathione, Iron, Recombinant Proteins, Saccharomyces cerevisiae Proteins, Sulfur.
- chemical , genetics : Glutaredoxins, Recombinant Proteins, Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Coordination Complexes, Glutaredoxins, Glutathione, Iron, Recombinant Proteins, Saccharomyces cerevisiae Proteins, Sulfur.
- chemistry : Plasmids, Saccharomyces cerevisiae.
- enzymology : Saccharomyces cerevisiae.
- genetics : Escherichia coli.
- metabolism : Escherichia coli, Plasmids.
- Amino Acid Sequence, Catalytic Domain, Cloning, Molecular, Crystallography, X-Ray, Gene Expression, Models, Molecular, Protein Binding, Protein Conformation, alpha-Helical, Protein Conformation, beta-Strand, Protein Interaction Domains and Motifs, Protein Multimerization, Sequence Alignment, Sequence Homology, Amino Acid.

Abstract

Glutaredoxins (Grxs) constitute a superfamily of proteins that perform diverse biological functions. The Saccharomyces cerevisiae glutaredoxin Grx6 not only serves as a glutathione (GSH)-dependent oxidoreductase and as a GSH transferase, but also as an essential [2Fe-2S]-binding protein. Here, the dimeric structure of the C-terminal domain of Grx6 (holo Grx6C), bridged by one [2Fe-2S] cluster coordinated by the active-site Cys136 and two external GSH molecules, is reported. Structural comparison combined with multiple-sequence alignment demonstrated that holo Grx6C is similar to the [2Fe-2S] cluster-incorporated dithiol Grxs, which share a highly conserved [2Fe-2S] cluster-binding pattern and dimeric conformation that is distinct from the previously identified [2Fe-2S] cluster-ligated monothiol Grxs.

DOI: 10.1107/S2053230X16013418
PubMed: 27710937
PubMed Central: PMC5053157

Affiliations:

République populaire de Chine

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 000402
to stream Main, to step Curation: 000402

Le document en format XML

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<author><name sortKey="Cheng, Wang" sort="Cheng, Wang" uniqKey="Cheng W" first="Wang" last="Cheng">Wang Cheng</name>
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<author><name sortKey="Cao, Dong Dong" sort="Cao, Dong Dong" uniqKey="Cao D" first="Dong Dong" last="Cao">Dong Dong Cao</name>
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<author><name sortKey="Zhou, Kang" sort="Zhou, Kang" uniqKey="Zhou K" first="Kang" last="Zhou">Kang Zhou</name>
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<author><name sortKey="Ali, Wafa" sort="Ali, Wafa" uniqKey="Ali W" first="Wafa" last="Ali">Wafa Ali</name>
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<author><name sortKey="Chen, Yuxing" sort="Chen, Yuxing" uniqKey="Chen Y" first="Yuxing" last="Chen">Yuxing Chen</name>
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<author><name sortKey="Zhou, Cong Zhao" sort="Zhou, Cong Zhao" uniqKey="Zhou C" first="Cong Zhao" last="Zhou">Cong Zhao Zhou</name>
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<term>Catalytic Domain (MeSH)</term>
<term>Cloning, Molecular (MeSH)</term>
<term>Coordination Complexes (chemistry)</term>
<term>Coordination Complexes (metabolism)</term>
<term>Crystallography, X-Ray (MeSH)</term>
<term>Escherichia coli (genetics)</term>
<term>Escherichia coli (metabolism)</term>
<term>Gene Expression (MeSH)</term>
<term>Glutaredoxins (chemistry)</term>
<term>Glutaredoxins (genetics)</term>
<term>Glutaredoxins (metabolism)</term>
<term>Glutathione (chemistry)</term>
<term>Glutathione (metabolism)</term>
<term>Iron (chemistry)</term>
<term>Iron (metabolism)</term>
<term>Models, Molecular (MeSH)</term>
<term>Plasmids (chemistry)</term>
<term>Plasmids (metabolism)</term>
<term>Protein Binding (MeSH)</term>
<term>Protein Conformation, alpha-Helical (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>Sequence Alignment (MeSH)</term>
<term>Sequence Homology, Amino Acid (MeSH)</term>
<term>Sulfur (chemistry)</term>
<term>Sulfur (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences (MeSH)</term>
<term>Clonage moléculaire (MeSH)</term>
<term>Complexes de coordination (composition chimique)</term>
<term>Complexes de coordination (métabolisme)</term>
<term>Cristallographie aux rayons X (MeSH)</term>
<term>Domaine catalytique (MeSH)</term>
<term>Escherichia coli (génétique)</term>
<term>Escherichia coli (métabolisme)</term>
<term>Expression des gènes (MeSH)</term>
<term>Fer (composition chimique)</term>
<term>Fer (métabolisme)</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>Plasmides (composition chimique)</term>
<term>Plasmides (métabolisme)</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>Saccharomyces cerevisiae (composition chimique)</term>
<term>Saccharomyces cerevisiae (enzymologie)</term>
<term>Similitude de séquences d'acides aminés (MeSH)</term>
<term>Soufre (composition chimique)</term>
<term>Soufre (métabolisme)</term>
<term>Structure en brin bêta (MeSH)</term>
<term>Structure en hélice alpha (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Coordination Complexes</term>
<term>Glutaredoxins</term>
<term>Glutathione</term>
<term>Iron</term>
<term>Recombinant Proteins</term>
<term>Saccharomyces cerevisiae Proteins</term>
<term>Sulfur</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glutaredoxins</term>
<term>Recombinant Proteins</term>
<term>Saccharomyces cerevisiae Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Coordination Complexes</term>
<term>Glutaredoxins</term>
<term>Glutathione</term>
<term>Iron</term>
<term>Recombinant Proteins</term>
<term>Saccharomyces cerevisiae Proteins</term>
<term>Sulfur</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Plasmids</term>
<term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Complexes de coordination</term>
<term>Fer</term>
<term>Glutarédoxines</term>
<term>Glutathion</term>
<term>Plasmides</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Protéines recombinantes</term>
<term>Saccharomyces cerevisiae</term>
<term>Soufre</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>
</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>Plasmids</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Complexes de coordination</term>
<term>Escherichia coli</term>
<term>Fer</term>
<term>Glutarédoxines</term>
<term>Glutathion</term>
<term>Plasmides</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Protéines recombinantes</term>
<term>Soufre</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>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>Sequence Alignment</term>
<term>Sequence Homology, Amino Acid</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term>
<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>Similitude de séquences d'acides aminés</term>
<term>Structure en brin bêta</term>
<term>Structure en hélice alpha</term>
<term>Séquence d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">Glutaredoxins (Grxs) constitute a superfamily of proteins that perform diverse biological functions. The Saccharomyces cerevisiae glutaredoxin Grx6 not only serves as a glutathione (GSH)-dependent oxidoreductase and as a GSH transferase, but also as an essential [2Fe-2S]-binding protein. Here, the dimeric structure of the C-terminal domain of Grx6 (holo Grx6C), bridged by one [2Fe-2S] cluster coordinated by the active-site Cys136 and two external GSH molecules, is reported. Structural comparison combined with multiple-sequence alignment demonstrated that holo Grx6C is similar to the [2Fe-2S] cluster-incorporated dithiol Grxs, which share a highly conserved [2Fe-2S] cluster-binding pattern and dimeric conformation that is distinct from the previously identified [2Fe-2S] cluster-ligated monothiol Grxs.</div>
</front>
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<DateCompleted><Year>2017</Year>
<Month>11</Month>
<Day>24</Day>
</DateCompleted>
<DateRevised><Year>2019</Year>
<Month>01</Month>
<Day>12</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">2053-230X</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>72</Volume>
<Issue>Pt 10</Issue>
<PubDate><Year>2016</Year>
<Month>10</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>Crystal structure of yeast monothiol glutaredoxin Grx6 in complex with a glutathione-coordinated [2Fe-2S] cluster.</ArticleTitle>
<Pagination><MedlinePgn>732-737</MedlinePgn>
</Pagination>
<Abstract><AbstractText>Glutaredoxins (Grxs) constitute a superfamily of proteins that perform diverse biological functions. The Saccharomyces cerevisiae glutaredoxin Grx6 not only serves as a glutathione (GSH)-dependent oxidoreductase and as a GSH transferase, but also as an essential [2Fe-2S]-binding protein. Here, the dimeric structure of the C-terminal domain of Grx6 (holo Grx6C), bridged by one [2Fe-2S] cluster coordinated by the active-site Cys136 and two external GSH molecules, is reported. Structural comparison combined with multiple-sequence alignment demonstrated that holo Grx6C is similar to the [2Fe-2S] cluster-incorporated dithiol Grxs, which share a highly conserved [2Fe-2S] cluster-binding pattern and dimeric conformation that is distinct from the previously identified [2Fe-2S] cluster-ligated monothiol Grxs.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Abdalla</LastName>
<ForeName>Mohnad</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230027, People's Republic of China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Dai</LastName>
<ForeName>Ya Nan</ForeName>
<Initials>YN</Initials>
<AffiliationInfo><Affiliation>Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230027, People's Republic of China.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Chi</LastName>
<ForeName>Chang Biao</ForeName>
<Initials>CB</Initials>
<AffiliationInfo><Affiliation>Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230027, People's Republic of China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Cheng</LastName>
<ForeName>Wang</ForeName>
<Initials>W</Initials>
<AffiliationInfo><Affiliation>Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230027, People's Republic of China.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Cao</LastName>
<ForeName>Dong Dong</ForeName>
<Initials>DD</Initials>
<AffiliationInfo><Affiliation>Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230027, People's Republic of China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Zhou</LastName>
<ForeName>Kang</ForeName>
<Initials>K</Initials>
<AffiliationInfo><Affiliation>Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230027, People's Republic of China.</Affiliation>
</AffiliationInfo>
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<ForeName>Wafa</ForeName>
<Initials>W</Initials>
<AffiliationInfo><Affiliation>Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230027, People's Republic of China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Chen</LastName>
<ForeName>Yuxing</ForeName>
<Initials>Y</Initials>
<AffiliationInfo><Affiliation>Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230027, People's Republic of China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Zhou</LastName>
<ForeName>Cong Zhao</ForeName>
<Initials>CZ</Initials>
<AffiliationInfo><Affiliation>Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230027, People's Republic of China.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2016</Year>
<Month>09</Month>
<Day>22</Day>
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<MedlineTA>Acta Crystallogr F Struct Biol Commun</MedlineTA>
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<ISSNLinking>2053-230X</ISSNLinking>
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<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="D056831" MajorTopicYN="N">Coordination Complexes</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName>
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<MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
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<MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName>
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<Keyword MajorTopicYN="Y">glutaredoxin</Keyword>
<Keyword MajorTopicYN="Y">iron–sulfur cluster</Keyword>
<Keyword MajorTopicYN="Y">oxidoreductase</Keyword>
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<affiliations><list><country><li>République populaire de Chine</li>
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Crystal structure of yeast monothiol glutaredoxin Grx6 in complex with a glutathione-coordinated [2Fe-2S] cluster.

Crystal structure of yeast monothiol glutaredoxin Grx6 in complex with a glutathione-coordinated [2Fe-2S] cluster.

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