Crystal structure of spinach plastocyanin at 1.7 A resolution.
Identifieur interne : 004944 ( Main/Corpus ); précédent : 004943; suivant : 004945Crystal structure of spinach plastocyanin at 1.7 A resolution.
Auteurs : Y. Xue ; M. Okvist ; O. Hansson ; S. YoungSource :
- Protein science : a publication of the Protein Society [ 0961-8368 ] ; 1998.
English descriptors
- KwdEn :
- 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
Links to Exploration step
pubmed:9792096Le 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>
<affiliation><nlm:affiliation>Department of Chemistry, Biochemistry and Biophysics, Göteborg University, Sweden. Yafeng.Xue@hassle.se.astra.com</nlm:affiliation>
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<author><name sortKey="Okvist, M" sort="Okvist, M" uniqKey="Okvist M" first="M" last="Okvist">M. Okvist</name>
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<author><name sortKey="Hansson, O" sort="Hansson, O" uniqKey="Hansson O" first="O" last="Hansson">O. Hansson</name>
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<author><name sortKey="Young, S" sort="Young, S" uniqKey="Young S" first="S" last="Young">S. Young</name>
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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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<author><name sortKey="Okvist, M" sort="Okvist, M" uniqKey="Okvist M" first="M" last="Okvist">M. Okvist</name>
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<author><name sortKey="Hansson, O" sort="Hansson, O" uniqKey="Hansson O" first="O" last="Hansson">O. Hansson</name>
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<author><name sortKey="Young, S" sort="Young, S" uniqKey="Young S" first="S" last="Young">S. Young</name>
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<series><title level="j">Protein science : a publication of the Protein Society</title>
<idno type="ISSN">0961-8368</idno>
<imprint><date when="1998" type="published">1998</date>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Binding Sites (MeSH)</term>
<term>Copper (metabolism)</term>
<term>Crystallization (MeSH)</term>
<term>Crystallography, X-Ray (MeSH)</term>
<term>Models, Molecular (MeSH)</term>
<term>Mutagenesis, Site-Directed (genetics)</term>
<term>Plastocyanin (chemistry)</term>
<term>Protein Structure, Tertiary (MeSH)</term>
<term>Spinacia oleracea (chemistry)</term>
<term>Static Electricity (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Plastocyanin</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Copper</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Spinacia oleracea</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Mutagenesis, Site-Directed</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term>
<term>Crystallization</term>
<term>Crystallography, X-Ray</term>
<term>Models, Molecular</term>
<term>Protein Structure, Tertiary</term>
<term>Static Electricity</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>
</front>
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<Abstract><AbstractText>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.</AbstractText>
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