The structure of a reduced mutant T4 glutaredoxin.
Identifieur interne : 001210 ( Main/Exploration ); précédent : 001209; suivant : 001211The structure of a reduced mutant T4 glutaredoxin.
Auteurs : M. Ingelman [Suède] ; P. Nordlund ; H. EklundSource :
- FEBS letters [ 0014-5793 ] ; 1995.
Descripteurs français
- KwdFr :
- Bactériophage T4 (composition chimique), Bactériophage T4 (génétique), Conformation des protéines (MeSH), Cristallographie (MeSH), Glutarédoxines (MeSH), Mutation (MeSH), Oxidoreductases (MeSH), Proline (composition chimique), Proline (génétique), Protéines (composition chimique), Protéines (génétique), Tyrosine (composition chimique), Tyrosine (génétique), Valine (composition chimique), Valine (génétique).
- MESH :
- composition chimique : Bactériophage T4, Proline, Protéines, Tyrosine, Valine.
- génétique : Bactériophage T4, Proline, Protéines, Tyrosine, Valine.
- Conformation des protéines, Cristallographie, Glutarédoxines, Mutation, Oxidoreductases.
English descriptors
- KwdEn :
- Bacteriophage T4 (chemistry), Bacteriophage T4 (genetics), Crystallography (MeSH), Glutaredoxins (MeSH), Mutation (MeSH), Oxidoreductases (MeSH), Proline (chemistry), Proline (genetics), Protein Conformation (MeSH), Proteins (chemistry), Proteins (genetics), Tyrosine (chemistry), Tyrosine (genetics), Valine (chemistry), Valine (genetics).
- MESH :
- chemical , chemistry : Proline, Proteins, Tyrosine, Valine.
- chemical , genetics : Proline, Proteins, Tyrosine, Valine.
- chemical : Glutaredoxins, Oxidoreductases.
- chemistry : Bacteriophage T4.
- genetics : Bacteriophage T4.
- Crystallography, Mutation, Protein Conformation.
Abstract
The mutant T4 glutaredoxin where the active site residues Val15 and Tyr16 have been substituted by Gly and Pro, respectively, crystallizes in a form where the active site disulfide is accessible to reagents. Treatment of the crystals with dithiotreitol causes very subtle changes in the overall glutaredoxin structure. The main differences are seen around the active site where the sulfurs of Cys14 and Cys17 move apart slightly.
DOI: 10.1016/0014-5793(95)00806-k
PubMed: 7656978
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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<affiliation wicri:level="1"><nlm:affiliation>Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala, Sweden.</nlm:affiliation>
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<author><name sortKey="Nordlund, P" sort="Nordlund, P" uniqKey="Nordlund P" first="P" last="Nordlund">P. Nordlund</name>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Bacteriophage T4 (chemistry)</term>
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<term>Crystallography (MeSH)</term>
<term>Glutaredoxins (MeSH)</term>
<term>Mutation (MeSH)</term>
<term>Oxidoreductases (MeSH)</term>
<term>Proline (chemistry)</term>
<term>Proline (genetics)</term>
<term>Protein Conformation (MeSH)</term>
<term>Proteins (chemistry)</term>
<term>Proteins (genetics)</term>
<term>Tyrosine (chemistry)</term>
<term>Tyrosine (genetics)</term>
<term>Valine (chemistry)</term>
<term>Valine (genetics)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Bactériophage T4 (composition chimique)</term>
<term>Bactériophage T4 (génétique)</term>
<term>Conformation des protéines (MeSH)</term>
<term>Cristallographie (MeSH)</term>
<term>Glutarédoxines (MeSH)</term>
<term>Mutation (MeSH)</term>
<term>Oxidoreductases (MeSH)</term>
<term>Proline (composition chimique)</term>
<term>Proline (génétique)</term>
<term>Protéines (composition chimique)</term>
<term>Protéines (génétique)</term>
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<term>Tyrosine (génétique)</term>
<term>Valine (composition chimique)</term>
<term>Valine (génétique)</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Proline</term>
<term>Proteins</term>
<term>Tyrosine</term>
<term>Valine</term>
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<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Proline</term>
<term>Proteins</term>
<term>Tyrosine</term>
<term>Valine</term>
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<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Glutaredoxins</term>
<term>Oxidoreductases</term>
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<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Bacteriophage T4</term>
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<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Bactériophage T4</term>
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<term>Protéines</term>
<term>Tyrosine</term>
<term>Valine</term>
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<front><div type="abstract" xml:lang="en">The mutant T4 glutaredoxin where the active site residues Val15 and Tyr16 have been substituted by Gly and Pro, respectively, crystallizes in a form where the active site disulfide is accessible to reagents. Treatment of the crystals with dithiotreitol causes very subtle changes in the overall glutaredoxin structure. The main differences are seen around the active site where the sulfurs of Cys14 and Cys17 move apart slightly.</div>
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<Day>21</Day>
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<Title>FEBS letters</Title>
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<ArticleTitle>The structure of a reduced mutant T4 glutaredoxin.</ArticleTitle>
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<Abstract><AbstractText>The mutant T4 glutaredoxin where the active site residues Val15 and Tyr16 have been substituted by Gly and Pro, respectively, crystallizes in a form where the active site disulfide is accessible to reagents. Treatment of the crystals with dithiotreitol causes very subtle changes in the overall glutaredoxin structure. The main differences are seen around the active site where the sulfurs of Cys14 and Cys17 move apart slightly.</AbstractText>
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