The 2.15 A crystal structure of a triple mutant plastocyanin from the cyanobacterium Synechocystis sp. PCC 6803.
Identifieur interne : 004915 ( Main/Exploration ); précédent : 004914; suivant : 004916The 2.15 A crystal structure of a triple mutant plastocyanin from the cyanobacterium Synechocystis sp. PCC 6803.
Auteurs : A. Romero [Espagne] ; B. De La Cerda ; P F Varela ; J A Navarro ; M. Hervás ; M A De La RosaSource :
- Journal of molecular biology [ 0022-2836 ] ; 1998.
Descripteurs français
- KwdFr :
- Alignement de séquences (MeSH), Animaux (MeSH), Arbres (MeSH), Chlamydomonas reinhardtii (MeSH), Cinétique (MeSH), Conformation des protéines (MeSH), Cristallographie aux rayons X (MeSH), Cyanobactéries (métabolisme), Données de séquences moléculaires (MeSH), Modèles moléculaires (MeSH), Mutagenèse dirigée (MeSH), Mutation ponctuelle (MeSH), Plastocyanine (composition chimique), Plastocyanine (métabolisme), Pliage des protéines (MeSH), Protéines recombinantes (composition chimique), Similitude de séquences d'acides aminés (MeSH), Structure secondaire des protéines (MeSH), Séquence d'acides aminés (MeSH), Électricité statique (MeSH).
- MESH :
- composition chimique : Plastocyanine, Protéines recombinantes.
- métabolisme : Cyanobactéries, Plastocyanine.
- Alignement de séquences, Animaux, Arbres, Chlamydomonas reinhardtii, Cinétique, Conformation des protéines, Cristallographie aux rayons X, Données de séquences moléculaires, Modèles moléculaires, Mutagenèse dirigée, Mutation ponctuelle, Pliage des protéines, Similitude de séquences d'acides aminés, Structure secondaire des protéines, Séquence d'acides aminés, Électricité statique.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Animals (MeSH), Chlamydomonas reinhardtii (MeSH), Crystallography, X-Ray (MeSH), Cyanobacteria (metabolism), Kinetics (MeSH), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Mutagenesis, Site-Directed (MeSH), Plastocyanin (chemistry), Plastocyanin (metabolism), Point Mutation (MeSH), Protein Conformation (MeSH), Protein Folding (MeSH), Protein Structure, Secondary (MeSH), Recombinant Proteins (chemistry), Sequence Alignment (MeSH), Sequence Homology, Amino Acid (MeSH), Static Electricity (MeSH), Trees (MeSH).
- MESH :
- chemical , chemistry : Plastocyanin, Recombinant Proteins.
- metabolism : Cyanobacteria, Plastocyanin.
- Amino Acid Sequence, Animals, Chlamydomonas reinhardtii, Crystallography, X-Ray, Kinetics, Models, Molecular, Molecular Sequence Data, Mutagenesis, Site-Directed, Point Mutation, Protein Conformation, Protein Folding, Protein Structure, Secondary, Sequence Alignment, Sequence Homology, Amino Acid, Static Electricity, Trees.
Abstract
The crystal structure of the triple mutant A42D/D47P/A63L plastocyanin from the cyanobacterium Synechocystis sp. PCC 6803 has been determined by Patterson search methods using the known structure of the poplar protein. Crystals of the triple mutant A42D/D47P/A63L, which are stable for days in its oxidized form, were grown from ammonium sulfate, with the cell constants a = b = 34.3 A and c = 111.8 A belonging to space group P3(2)21. The structure was refined using restrained crystallographic refinement to an R-factor of 16.7% for 4070 independent reflections between 8.0 and 2.15 A with intensities greater than 2 sigma (I), with root mean square deviations of 0.013 A and 1.63 degrees from ideal bond lengths and bond angles, respectively. The final model comprises 727 non-hydrogen protein atoms within 98 residues, 75 water molecules and a single copper ion. The overall tertiary fold of Synechocystis plastocyanin consists of a compact ellipsoidal beta-sandwich structure made up of two beta-sheets embracing a hydrophobic core. Each sheet contains parallel and antiparallel beta-strands. In addition to the beta-sheets, the structure contains an alpha-helix from Pro47 to Lys54 that follows beta-strand 4. The three-dimensional structure of Synechocystis plastocyanin is thus similar to those reported for the copper protein isolated from eukaryotic organisms and, in particular, from the cyanobacterium Anabaena variabilis, the only cyanobacterial plastocyanin structure available so far. The molecule holds an hydrophobic region surrounding His87, as do other plastocyanins, but the lack of negatively charged residues at the putative distant remote site surrounding Tyr83 could explain why the Synechocystis protein exhibits a collisional reaction mechanism for electron transfer to photosystem I (PSI), which involves no formation of the transient plastocyanin-PSI complex kinetically observed in green algae and higher plants.
DOI: 10.1006/jmbi.1997.1455
PubMed: 9466912
Affiliations:
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De La Cerda</name></author><author><name sortKey="Varela, P F" sort="Varela, P F" uniqKey="Varela P" first="P F" last="Varela">P F Varela</name></author><author><name sortKey="Navarro, J A" sort="Navarro, J A" uniqKey="Navarro J" first="J A" last="Navarro">J A Navarro</name></author><author><name sortKey="Hervas, M" sort="Hervas, M" uniqKey="Hervas M" first="M" last="Hervás">M. Hervás</name></author><author><name sortKey="De La Rosa, M A" sort="De La Rosa, M A" uniqKey="De La Rosa M" first="M A" last="De La Rosa">M A De La Rosa</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1998">1998</date><idno type="RBID">pubmed:9466912</idno><idno type="pmid">9466912</idno><idno type="doi">10.1006/jmbi.1997.1455</idno><idno type="wicri:Area/Main/Corpus">004966</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">004966</idno><idno type="wicri:Area/Main/Curation">004966</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">004966</idno><idno type="wicri:Area/Main/Exploration">004966</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The 2.15 A crystal structure of a triple mutant plastocyanin from the cyanobacterium Synechocystis sp. PCC 6803.</title><author><name sortKey="Romero, A" sort="Romero, A" uniqKey="Romero A" first="A" last="Romero">A. Romero</name><affiliation wicri:level="3"><nlm:affiliation>Centro de Investigaciones Biológicas, CSIC, Madrid, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Centro de Investigaciones Biológicas, CSIC, Madrid</wicri:regionArea><placeName><settlement type="city">Madrid</settlement><region nuts="2" type="region">Communauté de Madrid</region></placeName></affiliation></author><author><name sortKey="De La Cerda, B" sort="De La Cerda, B" uniqKey="De La Cerda B" first="B" last="De La Cerda">B. De La Cerda</name></author><author><name sortKey="Varela, P F" sort="Varela, P F" uniqKey="Varela P" first="P F" last="Varela">P F Varela</name></author><author><name sortKey="Navarro, J A" sort="Navarro, J A" uniqKey="Navarro J" first="J A" last="Navarro">J A Navarro</name></author><author><name sortKey="Hervas, M" sort="Hervas, M" uniqKey="Hervas M" first="M" last="Hervás">M. Hervás</name></author><author><name sortKey="De La Rosa, M A" sort="De La Rosa, M A" uniqKey="De La Rosa M" first="M A" last="De La Rosa">M A De La Rosa</name></author></analytic><series><title level="j">Journal of molecular biology</title><idno type="ISSN">0022-2836</idno><imprint><date when="1998" type="published">1998</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Animals (MeSH)</term><term>Chlamydomonas reinhardtii (MeSH)</term><term>Crystallography, X-Ray (MeSH)</term><term>Cyanobacteria (metabolism)</term><term>Kinetics (MeSH)</term><term>Models, Molecular (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Mutagenesis, Site-Directed (MeSH)</term><term>Plastocyanin (chemistry)</term><term>Plastocyanin (metabolism)</term><term>Point Mutation (MeSH)</term><term>Protein Conformation (MeSH)</term><term>Protein Folding (MeSH)</term><term>Protein Structure, Secondary (MeSH)</term><term>Recombinant Proteins (chemistry)</term><term>Sequence Alignment (MeSH)</term><term>Sequence Homology, Amino Acid (MeSH)</term><term>Static Electricity (MeSH)</term><term>Trees (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences (MeSH)</term><term>Animaux (MeSH)</term><term>Arbres (MeSH)</term><term>Chlamydomonas reinhardtii (MeSH)</term><term>Cinétique (MeSH)</term><term>Conformation des protéines (MeSH)</term><term>Cristallographie aux rayons X (MeSH)</term><term>Cyanobactéries (métabolisme)</term><term>Données de séquences moléculaires (MeSH)</term><term>Modèles moléculaires (MeSH)</term><term>Mutagenèse dirigée (MeSH)</term><term>Mutation ponctuelle (MeSH)</term><term>Plastocyanine (composition chimique)</term><term>Plastocyanine (métabolisme)</term><term>Pliage des protéines (MeSH)</term><term>Protéines recombinantes (composition chimique)</term><term>Similitude de séquences d'acides aminés (MeSH)</term><term>Structure secondaire des protéines (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Électricité statique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Plastocyanin</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Plastocyanine</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cyanobacteria</term><term>Plastocyanin</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cyanobactéries</term><term>Plastocyanine</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Chlamydomonas reinhardtii</term><term>Crystallography, X-Ray</term><term>Kinetics</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Mutagenesis, Site-Directed</term><term>Point Mutation</term><term>Protein Conformation</term><term>Protein Folding</term><term>Protein Structure, Secondary</term><term>Sequence Alignment</term><term>Sequence Homology, Amino Acid</term><term>Static Electricity</term><term>Trees</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Animaux</term><term>Arbres</term><term>Chlamydomonas reinhardtii</term><term>Cinétique</term><term>Conformation des protéines</term><term>Cristallographie aux rayons X</term><term>Données de séquences moléculaires</term><term>Modèles moléculaires</term><term>Mutagenèse dirigée</term><term>Mutation ponctuelle</term><term>Pliage des protéines</term><term>Similitude de séquences d'acides aminés</term><term>Structure secondaire des protéines</term><term>Séquence d'acides aminés</term><term>Électricité statique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The crystal structure of the triple mutant A42D/D47P/A63L plastocyanin from the cyanobacterium Synechocystis sp. PCC 6803 has been determined by Patterson search methods using the known structure of the poplar protein. Crystals of the triple mutant A42D/D47P/A63L, which are stable for days in its oxidized form, were grown from ammonium sulfate, with the cell constants a = b = 34.3 A and c = 111.8 A belonging to space group P3(2)21. The structure was refined using restrained crystallographic refinement to an R-factor of 16.7% for 4070 independent reflections between 8.0 and 2.15 A with intensities greater than 2 sigma (I), with root mean square deviations of 0.013 A and 1.63 degrees from ideal bond lengths and bond angles, respectively. The final model comprises 727 non-hydrogen protein atoms within 98 residues, 75 water molecules and a single copper ion. The overall tertiary fold of Synechocystis plastocyanin consists of a compact ellipsoidal beta-sandwich structure made up of two beta-sheets embracing a hydrophobic core. Each sheet contains parallel and antiparallel beta-strands. In addition to the beta-sheets, the structure contains an alpha-helix from Pro47 to Lys54 that follows beta-strand 4. The three-dimensional structure of Synechocystis plastocyanin is thus similar to those reported for the copper protein isolated from eukaryotic organisms and, in particular, from the cyanobacterium Anabaena variabilis, the only cyanobacterial plastocyanin structure available so far. The molecule holds an hydrophobic region surrounding His87, as do other plastocyanins, but the lack of negatively charged residues at the putative distant remote site surrounding Tyr83 could explain why the Synechocystis protein exhibits a collisional reaction mechanism for electron transfer to photosystem I (PSI), which involves no formation of the transient plastocyanin-PSI complex kinetically observed in green algae and higher plants.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">9466912</PMID><DateCompleted><Year>1998</Year><Month>02</Month><Day>27</Day></DateCompleted><DateRevised><Year>2008</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0022-2836</ISSN><JournalIssue CitedMedium="Print"><Volume>275</Volume><Issue>2</Issue><PubDate><Year>1998</Year><Month>Jan</Month><Day>16</Day></PubDate></JournalIssue><Title>Journal of molecular biology</Title><ISOAbbreviation>J Mol Biol</ISOAbbreviation></Journal><ArticleTitle>The 2.15 A crystal structure of a triple mutant plastocyanin from the cyanobacterium Synechocystis sp. PCC 6803.</ArticleTitle><Pagination><MedlinePgn>327-36</MedlinePgn></Pagination><Abstract><AbstractText>The crystal structure of the triple mutant A42D/D47P/A63L plastocyanin from the cyanobacterium Synechocystis sp. PCC 6803 has been determined by Patterson search methods using the known structure of the poplar protein. Crystals of the triple mutant A42D/D47P/A63L, which are stable for days in its oxidized form, were grown from ammonium sulfate, with the cell constants a = b = 34.3 A and c = 111.8 A belonging to space group P3(2)21. The structure was refined using restrained crystallographic refinement to an R-factor of 16.7% for 4070 independent reflections between 8.0 and 2.15 A with intensities greater than 2 sigma (I), with root mean square deviations of 0.013 A and 1.63 degrees from ideal bond lengths and bond angles, respectively. The final model comprises 727 non-hydrogen protein atoms within 98 residues, 75 water molecules and a single copper ion. The overall tertiary fold of Synechocystis plastocyanin consists of a compact ellipsoidal beta-sandwich structure made up of two beta-sheets embracing a hydrophobic core. Each sheet contains parallel and antiparallel beta-strands. In addition to the beta-sheets, the structure contains an alpha-helix from Pro47 to Lys54 that follows beta-strand 4. The three-dimensional structure of Synechocystis plastocyanin is thus similar to those reported for the copper protein isolated from eukaryotic organisms and, in particular, from the cyanobacterium Anabaena variabilis, the only cyanobacterial plastocyanin structure available so far. The molecule holds an hydrophobic region surrounding His87, as do other plastocyanins, but the lack of negatively charged residues at the putative distant remote site surrounding Tyr83 could explain why the Synechocystis protein exhibits a collisional reaction mechanism for electron transfer to photosystem I (PSI), which involves no formation of the transient plastocyanin-PSI complex kinetically observed in green algae and higher plants.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Romero</LastName><ForeName>A</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Centro de Investigaciones Biológicas, CSIC, Madrid, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>De la Cerda</LastName><ForeName>B</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Varela</LastName><ForeName>P F</ForeName><Initials>PF</Initials></Author><Author ValidYN="Y"><LastName>Navarro</LastName><ForeName>J A</ForeName><Initials>JA</Initials></Author><Author ValidYN="Y"><LastName>Hervás</LastName><ForeName>M</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>De la Rosa</LastName><ForeName>M A</ForeName><Initials>MA</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D003160">Comparative Study</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>J Mol Biol</MedlineTA><NlmUniqueID>2985088R</NlmUniqueID><ISSNLinking>0022-2836</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>9014-09-9</RegistryNumber><NameOfSubstance UI="D010970">Plastocyanin</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016825" MajorTopicYN="N">Chlamydomonas reinhardtii</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000458" MajorTopicYN="N">Cyanobacteria</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016297" MajorTopicYN="N">Mutagenesis, Site-Directed</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010970" MajorTopicYN="N">Plastocyanin</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017354" MajorTopicYN="N">Point Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="Y">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017510" MajorTopicYN="Y">Protein Folding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017433" MajorTopicYN="N">Protein Structure, Secondary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055672" MajorTopicYN="N">Static Electricity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014197" MajorTopicYN="N">Trees</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1998</Year><Month>2</Month><Day>19</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1998</Year><Month>2</Month><Day>19</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1998</Year><Month>2</Month><Day>19</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">9466912</ArticleId><ArticleId IdType="pii">S0022-2836(97)91455-8</ArticleId><ArticleId IdType="doi">10.1006/jmbi.1997.1455</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Espagne</li></country><region><li>Communauté de Madrid</li></region><settlement><li>Madrid</li></settlement></list><tree><noCountry><name sortKey="De La Cerda, B" sort="De La Cerda, B" uniqKey="De La Cerda B" first="B" last="De La Cerda">B. De La Cerda</name><name sortKey="De La Rosa, M A" sort="De La Rosa, M A" uniqKey="De La Rosa M" first="M A" last="De La Rosa">M A De La Rosa</name><name sortKey="Hervas, M" sort="Hervas, M" uniqKey="Hervas M" first="M" last="Hervás">M. Hervás</name><name sortKey="Navarro, J A" sort="Navarro, J A" uniqKey="Navarro J" first="J A" last="Navarro">J A Navarro</name><name sortKey="Varela, P F" sort="Varela, P F" uniqKey="Varela P" first="P F" last="Varela">P F Varela</name></noCountry><country name="Espagne"><region name="Communauté de Madrid"><name sortKey="Romero, A" sort="Romero, A" uniqKey="Romero A" first="A" last="Romero">A. Romero</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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