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The structure of a reduced mutant T4 glutaredoxin.

Identifieur interne : 001210 ( Main/Exploration ); précédent : 001209; suivant : 001211

The structure of a reduced mutant T4 glutaredoxin.

Auteurs : M. Ingelman [Suède] ; P. Nordlund ; H. Eklund

Source :

RBID : pubmed:7656978

Descripteurs français

English descriptors

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:


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Le document en format XML

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<term>Glutaredoxins (MeSH)</term>
<term>Mutation (MeSH)</term>
<term>Oxidoreductases (MeSH)</term>
<term>Proline (chemistry)</term>
<term>Proline (genetics)</term>
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<term>Bactériophage T4 (composition chimique)</term>
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<term>Glutarédoxines (MeSH)</term>
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<term>Oxidoreductases (MeSH)</term>
<term>Proline (composition chimique)</term>
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<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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