The 1.6 A resolution crystal structure of a mutant plastocyanin bearing a 21-25 engineered disulfide bridge.
Identifieur interne : 004652 ( Main/Exploration ); précédent : 004651; suivant : 004653The 1.6 A resolution crystal structure of a mutant plastocyanin bearing a 21-25 engineered disulfide bridge.
Auteurs : M. Milani [Italie] ; L. Andolfi ; S. Cannistraro ; M P Verbeet ; M. BolognesiSource :
- Acta crystallographica. Section D, Biological crystallography [ 0907-4449 ] ; 2001.
Descripteurs français
- KwdFr :
- Arbres (composition chimique), Conformation des protéines (MeSH), Cristallisation (MeSH), Cristallographie aux rayons X (MeSH), Ingénierie des protéines (MeSH), Modèles moléculaires (MeSH), Mutation (MeSH), Plastocyanine (composition chimique), Plastocyanine (génétique), Protéines recombinantes (composition chimique).
- MESH :
- composition chimique : Arbres, Plastocyanine, Protéines recombinantes.
- génétique : Plastocyanine.
- Conformation des protéines, Cristallisation, Cristallographie aux rayons X, Ingénierie des protéines, Modèles moléculaires, Mutation.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Plastocyanin, Recombinant Proteins.
- chemical , genetics : Plastocyanin.
- chemistry : Trees.
- Crystallization, Crystallography, X-Ray, Models, Molecular, Mutation, Protein Conformation, Protein Engineering.
Abstract
Plastocyanin is an electron-transfer protein which has been largely used for biophysical studies as well as for protein-engineering experiments. A surface disulfide bridge has been engineered in poplar plastocyanin to allow protein chemisorption on gold substrates. The mutated plastocyanin crystal structure has been studied at 1.6 A resolution (R factor = 0.145, R(free) = 0.205) to characterize the effects of the engineered disulfide on the overall protein structure and on the Cu-coordination sphere in view of biophysical applications. The new orthorhombic crystal form isolated for the mutated plastocyanin displays two protein molecules per asymmetric unit.
DOI: 10.1107/s0907444901013221
PubMed: 11679761
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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<wicri:regionArea>Department of Physics-INFM, c/o Advanced Biotechnology Center-IST, University of Genova, Largo Rosanna Benzi 10, 16132 Genova</wicri:regionArea>
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<author><name sortKey="Cannistraro, S" sort="Cannistraro, S" uniqKey="Cannistraro S" first="S" last="Cannistraro">S. Cannistraro</name>
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<author><name sortKey="Verbeet, M P" sort="Verbeet, M P" uniqKey="Verbeet M" first="M P" last="Verbeet">M P Verbeet</name>
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<term>Mutation (MeSH)</term>
<term>Plastocyanin (chemistry)</term>
<term>Plastocyanin (genetics)</term>
<term>Protein Conformation (MeSH)</term>
<term>Protein Engineering (MeSH)</term>
<term>Recombinant Proteins (chemistry)</term>
<term>Trees (chemistry)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Arbres (composition chimique)</term>
<term>Conformation des protéines (MeSH)</term>
<term>Cristallisation (MeSH)</term>
<term>Cristallographie aux rayons X (MeSH)</term>
<term>Ingénierie des protéines (MeSH)</term>
<term>Modèles moléculaires (MeSH)</term>
<term>Mutation (MeSH)</term>
<term>Plastocyanine (composition chimique)</term>
<term>Plastocyanine (génétique)</term>
<term>Protéines recombinantes (composition chimique)</term>
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<term>Protéines recombinantes</term>
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<front><div type="abstract" xml:lang="en">Plastocyanin is an electron-transfer protein which has been largely used for biophysical studies as well as for protein-engineering experiments. A surface disulfide bridge has been engineered in poplar plastocyanin to allow protein chemisorption on gold substrates. The mutated plastocyanin crystal structure has been studied at 1.6 A resolution (R factor = 0.145, R(free) = 0.205) to characterize the effects of the engineered disulfide on the overall protein structure and on the Cu-coordination sphere in view of biophysical applications. The new orthorhombic crystal form isolated for the mutated plastocyanin displays two protein molecules per asymmetric unit.</div>
</front>
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<ArticleTitle>The 1.6 A resolution crystal structure of a mutant plastocyanin bearing a 21-25 engineered disulfide bridge.</ArticleTitle>
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<Abstract><AbstractText>Plastocyanin is an electron-transfer protein which has been largely used for biophysical studies as well as for protein-engineering experiments. A surface disulfide bridge has been engineered in poplar plastocyanin to allow protein chemisorption on gold substrates. The mutated plastocyanin crystal structure has been studied at 1.6 A resolution (R factor = 0.145, R(free) = 0.205) to characterize the effects of the engineered disulfide on the overall protein structure and on the Cu-coordination sphere in view of biophysical applications. The new orthorhombic crystal form isolated for the mutated plastocyanin displays two protein molecules per asymmetric unit.</AbstractText>
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