PoplarV1, Main, Exploration, bibRecord, 004954

Crystal structure of spinach plastocyanin at 1.7 A resolution.

Identifieur interne : 004954 ( Main/Exploration ); précédent : 004953; suivant : 004955

Crystal structure of spinach plastocyanin at 1.7 A resolution.

Auteurs : Y. Xue [Suède] ; M. Okvist ; O. Hansson ; S. Young

Source :

Protein science : a publication of the Protein Society [ 0961-8368 ] ; 1998.

RBID : pubmed:9792096

Descripteurs français

KwdFr :
- Cristallisation (MeSH), Cristallographie aux rayons X (MeSH), Cuivre (métabolisme), Modèles moléculaires (MeSH), Mutagenèse dirigée (génétique), Plastocyanine (composition chimique), Sites de fixation (MeSH), Spinacia oleracea (composition chimique), Structure tertiaire des protéines (MeSH), Électricité statique (MeSH).
MESH :
- composition chimique : Plastocyanine, Spinacia oleracea.
- génétique : Mutagenèse dirigée.
- métabolisme : Cuivre.
- Cristallisation, Cristallographie aux rayons X, Modèles moléculaires, Sites de fixation, Structure tertiaire des protéines, Électricité statique.

English descriptors

KwdEn :
- Binding Sites (MeSH), Copper (metabolism), Crystallization (MeSH), Crystallography, X-Ray (MeSH), Models, Molecular (MeSH), Mutagenesis, Site-Directed (genetics), Plastocyanin (chemistry), Protein Structure, Tertiary (MeSH), Spinacia oleracea (chemistry), Static Electricity (MeSH).
MESH :
- chemical , chemistry : Plastocyanin.
- chemical , metabolism : Copper.
- chemistry : Spinacia oleracea.
- genetics : Mutagenesis, Site-Directed.
- Binding Sites, Crystallization, Crystallography, X-Ray, Models, Molecular, Protein Structure, Tertiary, Static Electricity.

Abstract

The crystal structure of plastocyanin from spinach has been determined using molecular replacement, with the structure of plastocyanin from poplar as a search model. Successful crystallization was facilitated by site-directed mutagenesis in which residue Gly8 was substituted with Asp. The region around residue 8 was believed to be too mobile for the wild-type protein to form crystals despite extensive screening. The current structure represents the oxidized plastocyanin, copper (II), at low pH (approximately 4.4). In contrast to the similarity in the core region as compared to its poplar counterpart, the structure shows some significant differences in loop regions. The most notable is the large shift of the 59-61 loop where the largest shift is 3.0 A for the C(alpha) atom of Glu59. This results in different patterns of electrostatic potential around the acidic patches for the two proteins.

DOI: 10.1002/pro.5560071006
PubMed: 9792096
PubMed Central: PMC2143848

Affiliations:

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Le document en format XML

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<author><name sortKey="Xue, Y" sort="Xue, Y" uniqKey="Xue Y" first="Y" last="Xue">Y. Xue</name>
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<term>Models, Molecular (MeSH)</term>
<term>Mutagenesis, Site-Directed (genetics)</term>
<term>Plastocyanin (chemistry)</term>
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<term>Static Electricity (MeSH)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Cristallisation (MeSH)</term>
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<term>Cuivre (métabolisme)</term>
<term>Modèles moléculaires (MeSH)</term>
<term>Mutagenèse dirigée (génétique)</term>
<term>Plastocyanine (composition chimique)</term>
<term>Sites de fixation (MeSH)</term>
<term>Spinacia oleracea (composition chimique)</term>
<term>Structure tertiaire des protéines (MeSH)</term>
<term>Électricité statique (MeSH)</term>
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<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Spinacia oleracea</term>
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<term>Structure tertiaire des protéines</term>
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<front><div type="abstract" xml:lang="en">The crystal structure of plastocyanin from spinach has been determined using molecular replacement, with the structure of plastocyanin from poplar as a search model. Successful crystallization was facilitated by site-directed mutagenesis in which residue Gly8 was substituted with Asp. The region around residue 8 was believed to be too mobile for the wild-type protein to form crystals despite extensive screening. The current structure represents the oxidized plastocyanin, copper (II), at low pH (approximately 4.4). In contrast to the similarity in the core region as compared to its poplar counterpart, the structure shows some significant differences in loop regions. The most notable is the large shift of the 59-61 loop where the largest shift is 3.0 A for the C(alpha) atom of Glu59. This results in different patterns of electrostatic potential around the acidic patches for the two proteins.</div>
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Crystal structure of spinach plastocyanin at 1.7 A resolution.

Crystal structure of spinach plastocyanin at 1.7 A resolution.

Source :

Descripteurs français

English descriptors

Abstract

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

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki