PoplarV1, Main, Exploration, bibRecord, 004852

Structure comparison between oxidized and reduced plastocyanin from a fern, Dryopteris crassirhizoma.

Identifieur interne : 004852 ( Main/Exploration ); précédent : 004851; suivant : 004853

Structure comparison between oxidized and reduced plastocyanin from a fern, Dryopteris crassirhizoma.

Auteurs : T. Inoue [Japon] ; M. Gotowda ; H. Sugawara ; T. Kohzuma ; F. Yoshizaki ; Y. Sugimura ; Y. Kai

Source :

Biochemistry [ 0006-2960 ] ; 1999.

RBID : pubmed:10529231

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Aspartic Acid (chemistry), Binding Sites (MeSH), Chlorophyta (MeSH), Copper (chemistry), Copper (metabolism), Crystallography, X-Ray (MeSH), Cyanobacteria (MeSH), Glutamic Acid (chemistry), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Oxidation-Reduction (MeSH), Plants (chemistry), Plastocyanin (chemistry), Plastocyanin (metabolism), Protein Conformation (MeSH), Protein Structure, Secondary (MeSH), Species Specificity (MeSH), Trees (MeSH).
MESH :
- chemical , chemistry : Aspartic Acid, Copper, Glutamic Acid, Plastocyanin.
- chemical , metabolism : Copper, Plastocyanin.
- chemistry : Plants.
- Amino Acid Sequence, Binding Sites, Chlorophyta, Crystallography, X-Ray, Cyanobacteria, Models, Molecular, Molecular Sequence Data, Oxidation-Reduction, Protein Conformation, Protein Structure, Secondary, Species Specificity, Trees.

Abstract

The X-ray crystal structures of oxidized and reduced plastocyanin obtained from the fern Dryopteris crassirhizoma have been determined at 1.7 and 1.8 A resolution, respectively. The fern plastocyanin is unique in the longer main chain composed of 102 amino acid residues and in the unusual pH dependence due to the pi-pi stacking interaction around the copper site [Kohzuma, T., et al. (1999) J. Biol. Chem. 274, 11817-11823]. Here we report the structural comparison between the fern plastocyanin and other plastocyanins from cyanobacteria, green algae, and other higher plants, together with the structural changes of fern plastocyanin upon reduction. Glu59 hydrogen bonds to the OH of Tyr83, which is thought to be a possible conduit for electrons, in the oxidized state. However, it moves away from Tyr83 upon reduction like poplar plastocyanin.

DOI: 10.1021/bi990502t
PubMed: 10529231

Affiliations:

Japon

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Le document en format XML

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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term>
<term>Aspartic Acid (chemistry)</term>
<term>Binding Sites (MeSH)</term>
<term>Chlorophyta (MeSH)</term>
<term>Copper (chemistry)</term>
<term>Copper (metabolism)</term>
<term>Crystallography, X-Ray (MeSH)</term>
<term>Cyanobacteria (MeSH)</term>
<term>Glutamic Acid (chemistry)</term>
<term>Models, Molecular (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Plants (chemistry)</term>
<term>Plastocyanin (chemistry)</term>
<term>Plastocyanin (metabolism)</term>
<term>Protein Conformation (MeSH)</term>
<term>Protein Structure, Secondary (MeSH)</term>
<term>Species Specificity (MeSH)</term>
<term>Trees (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Acide aspartique (composition chimique)</term>
<term>Acide glutamique (composition chimique)</term>
<term>Arbres (MeSH)</term>
<term>Chlorophyta (MeSH)</term>
<term>Conformation des protéines (MeSH)</term>
<term>Cristallographie aux rayons X (MeSH)</term>
<term>Cuivre (composition chimique)</term>
<term>Cuivre (métabolisme)</term>
<term>Cyanobactéries (MeSH)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Modèles moléculaires (MeSH)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Plantes (composition chimique)</term>
<term>Plastocyanine (composition chimique)</term>
<term>Plastocyanine (métabolisme)</term>
<term>Sites de fixation (MeSH)</term>
<term>Spécificité d'espèce (MeSH)</term>
<term>Structure secondaire des protéines (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Aspartic Acid</term>
<term>Copper</term>
<term>Glutamic Acid</term>
<term>Plastocyanin</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Copper</term>
<term>Plastocyanin</term>
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<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Plants</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Acide aspartique</term>
<term>Acide glutamique</term>
<term>Cuivre</term>
<term>Plantes</term>
<term>Plastocyanine</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cuivre</term>
<term>Plastocyanine</term>
</keywords>
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<term>Binding Sites</term>
<term>Chlorophyta</term>
<term>Crystallography, X-Ray</term>
<term>Cyanobacteria</term>
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<term>Oxidation-Reduction</term>
<term>Protein Conformation</term>
<term>Protein Structure, Secondary</term>
<term>Species Specificity</term>
<term>Trees</term>
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<term>Chlorophyta</term>
<term>Conformation des protéines</term>
<term>Cristallographie aux rayons X</term>
<term>Cyanobactéries</term>
<term>Données de séquences moléculaires</term>
<term>Modèles moléculaires</term>
<term>Oxydoréduction</term>
<term>Sites de fixation</term>
<term>Spécificité d'espèce</term>
<term>Structure secondaire des protéines</term>
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<front><div type="abstract" xml:lang="en">The X-ray crystal structures of oxidized and reduced plastocyanin obtained from the fern Dryopteris crassirhizoma have been determined at 1.7 and 1.8 A resolution, respectively. The fern plastocyanin is unique in the longer main chain composed of 102 amino acid residues and in the unusual pH dependence due to the pi-pi stacking interaction around the copper site [Kohzuma, T., et al. (1999) J. Biol. Chem. 274, 11817-11823]. Here we report the structural comparison between the fern plastocyanin and other plastocyanins from cyanobacteria, green algae, and other higher plants, together with the structural changes of fern plastocyanin upon reduction. Glu59 hydrogen bonds to the OH of Tyr83, which is thought to be a possible conduit for electrons, in the oxidized state. However, it moves away from Tyr83 upon reduction like poplar plastocyanin.</div>
</front>
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<DateCompleted><Year>1999</Year>
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<ArticleTitle>Structure comparison between oxidized and reduced plastocyanin from a fern, Dryopteris crassirhizoma.</ArticleTitle>
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<Abstract><AbstractText>The X-ray crystal structures of oxidized and reduced plastocyanin obtained from the fern Dryopteris crassirhizoma have been determined at 1.7 and 1.8 A resolution, respectively. The fern plastocyanin is unique in the longer main chain composed of 102 amino acid residues and in the unusual pH dependence due to the pi-pi stacking interaction around the copper site [Kohzuma, T., et al. (1999) J. Biol. Chem. 274, 11817-11823]. Here we report the structural comparison between the fern plastocyanin and other plastocyanins from cyanobacteria, green algae, and other higher plants, together with the structural changes of fern plastocyanin upon reduction. Glu59 hydrogen bonds to the OH of Tyr83, which is thought to be a possible conduit for electrons, in the oxidized state. However, it moves away from Tyr83 upon reduction like poplar plastocyanin.</AbstractText>
</Abstract>
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Structure comparison between oxidized and reduced plastocyanin from a fern, Dryopteris crassirhizoma.

Structure comparison between oxidized and reduced plastocyanin from a fern, Dryopteris crassirhizoma.

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