The crystal structure of poplar apoplastocyanin at 1.8-A resolution. The geometry of the copper-binding site is created by the polypeptide.
Identifieur interne : 004E09 ( Main/Exploration ); précédent : 004E08; suivant : 004E10The crystal structure of poplar apoplastocyanin at 1.8-A resolution. The geometry of the copper-binding site is created by the polypeptide.
Auteurs : T P Garrett ; D J Clingeleffer ; J M Guss ; S J Rogers ; H C FreemanSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 1984.
Descripteurs français
- KwdFr :
- MESH :
- isolement et purification : Apoprotéines, Plastocyanine, Protéines végétales.
- Arbres, Conformation des protéines, Diffraction des rayons X, Modèles moléculaires.
English descriptors
- KwdEn :
- MESH :
- chemical , isolation & purification : Apoproteins, Plant Proteins, Plastocyanin.
- Models, Molecular, Protein Conformation, Trees, X-Ray Diffraction.
Abstract
The three-dimensional structure of apoplastocyanin from poplar leaves (Populus nigra var. italica) has been determined by x-ray diffraction at 1.8-A resolution. The structure closely resembles that of the holoprotein. In particular, the positions of the copper-binding residues in the apo- and holoproteins differ by only 0.1-0.3 A. This indicates that the irregular geometry of the "type 1" copper site is imposed upon the metal atom by the polypeptide moiety. A 180 degrees rotation of one solvent-exposed histidine imidazole ring about C beta-C gamma appears to facilitate access to the copper site. The close structural similarity between apo-, Cu-(II)-, and Cu(I)-plastocyanin was initially demonstrated by means of electron density difference maps. Two series of restrained least squares refinement calculations for apoplastocyanin, originating from different sets of atomic positional parameters, were carried out in parallel. Both refinements converged to the same model which, when fully refined, had a residual R = 0.16. Forty-two water molecules were located during the refinement.
DOI: 10.2210/pdb2pcy/pdb
PubMed: 6698995
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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The geometry of the copper-binding site is created by the polypeptide.</title><author><name sortKey="Garrett, T P" sort="Garrett, T P" uniqKey="Garrett T" first="T P" last="Garrett">T P Garrett</name></author><author><name sortKey="Clingeleffer, D J" sort="Clingeleffer, D J" uniqKey="Clingeleffer D" first="D J" last="Clingeleffer">D J Clingeleffer</name></author><author><name sortKey="Guss, J M" sort="Guss, J M" uniqKey="Guss J" first="J M" last="Guss">J M Guss</name></author><author><name sortKey="Rogers, S J" sort="Rogers, S J" uniqKey="Rogers S" first="S J" last="Rogers">S J Rogers</name></author><author><name sortKey="Freeman, H C" sort="Freeman, H C" uniqKey="Freeman H" first="H C" last="Freeman">H C Freeman</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1984">1984</date><idno type="RBID">pubmed:6698995</idno><idno type="pmid">6698995</idno><idno type="doi">10.2210/pdb2pcy/pdb</idno><idno type="wicri:Area/Main/Corpus">004E12</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">004E12</idno><idno type="wicri:Area/Main/Curation">004E12</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">004E12</idno><idno type="wicri:Area/Main/Exploration">004E12</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The crystal structure of poplar apoplastocyanin at 1.8-A resolution. The geometry of the copper-binding site is created by the polypeptide.</title><author><name sortKey="Garrett, T P" sort="Garrett, T P" uniqKey="Garrett T" first="T P" last="Garrett">T P Garrett</name></author><author><name sortKey="Clingeleffer, D J" sort="Clingeleffer, D J" uniqKey="Clingeleffer D" first="D J" last="Clingeleffer">D J Clingeleffer</name></author><author><name sortKey="Guss, J M" sort="Guss, J M" uniqKey="Guss J" first="J M" last="Guss">J M Guss</name></author><author><name sortKey="Rogers, S J" sort="Rogers, S J" uniqKey="Rogers S" first="S J" last="Rogers">S J Rogers</name></author><author><name sortKey="Freeman, H C" sort="Freeman, H C" uniqKey="Freeman H" first="H C" last="Freeman">H C Freeman</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="1984" type="published">1984</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Apoproteins (isolation & purification)</term><term>Models, Molecular (MeSH)</term><term>Plant Proteins (isolation & purification)</term><term>Plastocyanin (isolation & purification)</term><term>Protein Conformation (MeSH)</term><term>Trees (MeSH)</term><term>X-Ray Diffraction (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Apoprotéines (isolement et purification)</term><term>Arbres (MeSH)</term><term>Conformation des protéines (MeSH)</term><term>Diffraction des rayons X (MeSH)</term><term>Modèles moléculaires (MeSH)</term><term>Plastocyanine (isolement et purification)</term><term>Protéines végétales (isolement et purification)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Apoproteins</term><term>Plant Proteins</term><term>Plastocyanin</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Apoprotéines</term><term>Plastocyanine</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Models, Molecular</term><term>Protein Conformation</term><term>Trees</term><term>X-Ray Diffraction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Arbres</term><term>Conformation des protéines</term><term>Diffraction des rayons X</term><term>Modèles moléculaires</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The three-dimensional structure of apoplastocyanin from poplar leaves (Populus nigra var. italica) has been determined by x-ray diffraction at 1.8-A resolution. The structure closely resembles that of the holoprotein. In particular, the positions of the copper-binding residues in the apo- and holoproteins differ by only 0.1-0.3 A. This indicates that the irregular geometry of the "type 1" copper site is imposed upon the metal atom by the polypeptide moiety. A 180 degrees rotation of one solvent-exposed histidine imidazole ring about C beta-C gamma appears to facilitate access to the copper site. The close structural similarity between apo-, Cu-(II)-, and Cu(I)-plastocyanin was initially demonstrated by means of electron density difference maps. Two series of restrained least squares refinement calculations for apoplastocyanin, originating from different sets of atomic positional parameters, were carried out in parallel. Both refinements converged to the same model which, when fully refined, had a residual R = 0.16. Forty-two water molecules were located during the refinement.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">6698995</PMID><DateCompleted><Year>1984</Year><Month>04</Month><Day>24</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>08</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>259</Volume><Issue>5</Issue><PubDate><Year>1984</Year><Month>Mar</Month><Day>10</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>The crystal structure of poplar apoplastocyanin at 1.8-A resolution. The geometry of the copper-binding site is created by the polypeptide.</ArticleTitle><Pagination><MedlinePgn>2822-5</MedlinePgn></Pagination><Abstract><AbstractText>The three-dimensional structure of apoplastocyanin from poplar leaves (Populus nigra var. italica) has been determined by x-ray diffraction at 1.8-A resolution. The structure closely resembles that of the holoprotein. In particular, the positions of the copper-binding residues in the apo- and holoproteins differ by only 0.1-0.3 A. This indicates that the irregular geometry of the "type 1" copper site is imposed upon the metal atom by the polypeptide moiety. A 180 degrees rotation of one solvent-exposed histidine imidazole ring about C beta-C gamma appears to facilitate access to the copper site. The close structural similarity between apo-, Cu-(II)-, and Cu(I)-plastocyanin was initially demonstrated by means of electron density difference maps. Two series of restrained least squares refinement calculations for apoplastocyanin, originating from different sets of atomic positional parameters, were carried out in parallel. Both refinements converged to the same model which, when fully refined, had a residual R = 0.16. Forty-two water molecules were located during the refinement.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Garrett</LastName><ForeName>T P</ForeName><Initials>TP</Initials></Author><Author ValidYN="Y"><LastName>Clingeleffer</LastName><ForeName>D J</ForeName><Initials>DJ</Initials></Author><Author ValidYN="Y"><LastName>Guss</LastName><ForeName>J M</ForeName><Initials>JM</Initials></Author><Author ValidYN="Y"><LastName>Rogers</LastName><ForeName>S J</ForeName><Initials>SJ</Initials></Author><Author ValidYN="Y"><LastName>Freeman</LastName><ForeName>H C</ForeName><Initials>HC</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001059">Apoproteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C040778">apoplastocyanin</NameOfSubstance></Chemical><Chemical><RegistryNumber>9014-09-9</RegistryNumber><NameOfSubstance UI="D010970">Plastocyanin</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001059" MajorTopicYN="Y">Apoproteins</DescriptorName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="Y">Plant Proteins</DescriptorName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010970" MajorTopicYN="Y">Plastocyanin</DescriptorName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014197" MajorTopicYN="N">Trees</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014961" MajorTopicYN="N">X-Ray Diffraction</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1984</Year><Month>3</Month><Day>10</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1984</Year><Month>3</Month><Day>10</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1984</Year><Month>3</Month><Day>10</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">6698995</ArticleId><ArticleId IdType="doi">10.2210/pdb2pcy/pdb</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list></list><tree><noCountry><name sortKey="Clingeleffer, D J" sort="Clingeleffer, D J" uniqKey="Clingeleffer D" first="D J" last="Clingeleffer">D J Clingeleffer</name><name sortKey="Freeman, H C" sort="Freeman, H C" uniqKey="Freeman H" first="H C" last="Freeman">H C Freeman</name><name sortKey="Garrett, T P" sort="Garrett, T P" uniqKey="Garrett T" first="T P" last="Garrett">T P Garrett</name><name sortKey="Guss, J M" sort="Guss, J M" uniqKey="Guss J" first="J M" last="Guss">J M Guss</name><name sortKey="Rogers, S J" sort="Rogers, S J" uniqKey="Rogers S" first="S J" last="Rogers">S J Rogers</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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