Crystal structure of plastocyanin from a green alga, Enteromorpha prolifera.
Identifieur interne : 004C86 ( Main/Exploration ); précédent : 004C85; suivant : 004C87Crystal structure of plastocyanin from a green alga, Enteromorpha prolifera.
Auteurs : C A Collyer [Australie] ; J M Guss ; Y. Sugimura ; F. Yoshizaki ; H C FreemanSource :
- Journal of molecular biology [ 0022-2836 ] ; 1990.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , ultrastructure : Plant Proteins, Plastocyanin.
- chemical : Copper, Solvents.
- Amino Acid Sequence, Chlorophyta, Computer Graphics, Crystallography, Hydrogen Bonding, Models, Molecular, Molecular Sequence Data.
Abstract
The crystal structure of the Cu-containing protein plastocyanin (Mr 10,500) from the green alga Enteromorpha prolifera has been solved by molecular replacement. The structure was refined by constrained-restrained and restrained reciprocal space least-squares techniques. The refined model includes 111 solvent sites. There is evidence for alternate conformers at eight residues. The residual is 0.12 for a data set comprising 74% of all observations accessible at 1.85 A resolution. The beta-sandwich structure of the algal plastocyanin is effectively the same as that of poplar leaf (Populus nigra var. italica) plastocyanin determined at 1.6 A resolution. The sequence homology between the two proteins is 56%. Differences between the contacts in the hydrophobic core create some significant (0.5 to 1.2 A) movements of the polypeptide backbone, resulting in small differences between the orientations and separations of corresponding beta-strands. These differences are most pronounced at the end of the molecule remote from the Cu site. The largest structural differences occur in the single non-beta strand, which includes the sole turn of helix in the molecule: two of the residues in a prominent kink of the poplar plastocyanin backbone are missing from the algal plastocyanin sequence, and there is a significant change in the position of the helical segment in relation to the beta-sandwich. Several other small but significant structural differences can be correlated with intermolecular contacts in the crystals. An intramolecular carboxyl-carboxylate hydrogen bond in the algal plastocyanin may be associated with an unusually high pKa. The dimensions of the Cu site in the two plastocyanins are, within the limits of precision, identical.
DOI: 10.1016/0022-2836(90)90269-R
PubMed: 2308169
Affiliations:
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Sugimura</name></author><author><name sortKey="Yoshizaki, F" sort="Yoshizaki, F" uniqKey="Yoshizaki F" first="F" last="Yoshizaki">F. Yoshizaki</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="1990">1990</date><idno type="RBID">pubmed:2308169</idno><idno type="pmid">2308169</idno><idno type="doi">10.1016/0022-2836(90)90269-R</idno><idno type="wicri:Area/Main/Corpus">004C89</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">004C89</idno><idno type="wicri:Area/Main/Curation">004C89</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">004C89</idno><idno type="wicri:Area/Main/Exploration">004C89</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Crystal structure of plastocyanin from a green alga, Enteromorpha prolifera.</title><author><name sortKey="Collyer, C A" sort="Collyer, C A" uniqKey="Collyer C" first="C A" last="Collyer">C A Collyer</name><affiliation wicri:level="4"><nlm:affiliation>Department of Inorganic Chemistry, University of Sydney, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Department of Inorganic Chemistry, University of Sydney</wicri:regionArea><placeName><settlement type="city">Sydney</settlement><region type="état">Nouvelle-Galles du Sud</region></placeName><orgName type="university">Université de Sydney</orgName></affiliation></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="Sugimura, Y" sort="Sugimura, Y" uniqKey="Sugimura Y" first="Y" last="Sugimura">Y. Sugimura</name></author><author><name sortKey="Yoshizaki, F" sort="Yoshizaki, F" uniqKey="Yoshizaki F" first="F" last="Yoshizaki">F. Yoshizaki</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">Journal of molecular biology</title><idno type="ISSN">0022-2836</idno><imprint><date when="1990" type="published">1990</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Chlorophyta (MeSH)</term><term>Computer Graphics (MeSH)</term><term>Copper (MeSH)</term><term>Crystallography (MeSH)</term><term>Hydrogen Bonding (MeSH)</term><term>Models, Molecular (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Plant Proteins (ultrastructure)</term><term>Plastocyanin (ultrastructure)</term><term>Solvents (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Chlorophyta (MeSH)</term><term>Cristallographie (MeSH)</term><term>Cuivre (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Infographie (MeSH)</term><term>Liaison hydrogène (MeSH)</term><term>Modèles moléculaires (MeSH)</term><term>Plastocyanine (ultrastructure)</term><term>Protéines végétales (ultrastructure)</term><term>Solvants (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="ultrastructure" xml:lang="en"><term>Plant Proteins</term><term>Plastocyanin</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Copper</term><term>Solvents</term></keywords><keywords scheme="MESH" qualifier="ultrastructure" xml:lang="fr"><term>Plastocyanine</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Chlorophyta</term><term>Computer Graphics</term><term>Crystallography</term><term>Hydrogen Bonding</term><term>Models, Molecular</term><term>Molecular Sequence Data</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Chlorophyta</term><term>Cristallographie</term><term>Cuivre</term><term>Données de séquences moléculaires</term><term>Infographie</term><term>Liaison hydrogène</term><term>Modèles moléculaires</term><term>Solvants</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The crystal structure of the Cu-containing protein plastocyanin (Mr 10,500) from the green alga Enteromorpha prolifera has been solved by molecular replacement. The structure was refined by constrained-restrained and restrained reciprocal space least-squares techniques. The refined model includes 111 solvent sites. There is evidence for alternate conformers at eight residues. The residual is 0.12 for a data set comprising 74% of all observations accessible at 1.85 A resolution. The beta-sandwich structure of the algal plastocyanin is effectively the same as that of poplar leaf (Populus nigra var. italica) plastocyanin determined at 1.6 A resolution. The sequence homology between the two proteins is 56%. Differences between the contacts in the hydrophobic core create some significant (0.5 to 1.2 A) movements of the polypeptide backbone, resulting in small differences between the orientations and separations of corresponding beta-strands. These differences are most pronounced at the end of the molecule remote from the Cu site. The largest structural differences occur in the single non-beta strand, which includes the sole turn of helix in the molecule: two of the residues in a prominent kink of the poplar plastocyanin backbone are missing from the algal plastocyanin sequence, and there is a significant change in the position of the helical segment in relation to the beta-sandwich. Several other small but significant structural differences can be correlated with intermolecular contacts in the crystals. An intramolecular carboxyl-carboxylate hydrogen bond in the algal plastocyanin may be associated with an unusually high pKa. The dimensions of the Cu site in the two plastocyanins are, within the limits of precision, identical.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">2308169</PMID><DateCompleted><Year>1990</Year><Month>04</Month><Day>09</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0022-2836</ISSN><JournalIssue CitedMedium="Print"><Volume>211</Volume><Issue>3</Issue><PubDate><Year>1990</Year><Month>Feb</Month><Day>05</Day></PubDate></JournalIssue><Title>Journal of molecular biology</Title><ISOAbbreviation>J Mol Biol</ISOAbbreviation></Journal><ArticleTitle>Crystal structure of plastocyanin from a green alga, Enteromorpha prolifera.</ArticleTitle><Pagination><MedlinePgn>617-32</MedlinePgn></Pagination><Abstract><AbstractText>The crystal structure of the Cu-containing protein plastocyanin (Mr 10,500) from the green alga Enteromorpha prolifera has been solved by molecular replacement. The structure was refined by constrained-restrained and restrained reciprocal space least-squares techniques. The refined model includes 111 solvent sites. There is evidence for alternate conformers at eight residues. The residual is 0.12 for a data set comprising 74% of all observations accessible at 1.85 A resolution. The beta-sandwich structure of the algal plastocyanin is effectively the same as that of poplar leaf (Populus nigra var. italica) plastocyanin determined at 1.6 A resolution. The sequence homology between the two proteins is 56%. Differences between the contacts in the hydrophobic core create some significant (0.5 to 1.2 A) movements of the polypeptide backbone, resulting in small differences between the orientations and separations of corresponding beta-strands. These differences are most pronounced at the end of the molecule remote from the Cu site. The largest structural differences occur in the single non-beta strand, which includes the sole turn of helix in the molecule: two of the residues in a prominent kink of the poplar plastocyanin backbone are missing from the algal plastocyanin sequence, and there is a significant change in the position of the helical segment in relation to the beta-sandwich. Several other small but significant structural differences can be correlated with intermolecular contacts in the crystals. An intramolecular carboxyl-carboxylate hydrogen bond in the algal plastocyanin may be associated with an unusually high pKa. The dimensions of the Cu site in the two plastocyanins are, within the limits of precision, identical.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Collyer</LastName><ForeName>C A</ForeName><Initials>CA</Initials><AffiliationInfo><Affiliation>Department of Inorganic Chemistry, University of Sydney, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Guss</LastName><ForeName>J M</ForeName><Initials>JM</Initials></Author><Author ValidYN="Y"><LastName>Sugimura</LastName><ForeName>Y</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Yoshizaki</LastName><ForeName>F</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Freeman</LastName><ForeName>H C</ForeName><Initials>HC</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>PDB</DataBankName><AccessionNumberList><AccessionNumber>UNKNOWN</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><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="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012997">Solvents</NameOfSubstance></Chemical><Chemical><RegistryNumber>789U1901C5</RegistryNumber><NameOfSubstance UI="D003300">Copper</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="D000460" MajorTopicYN="N">Chlorophyta</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003196" MajorTopicYN="N">Computer Graphics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003300" MajorTopicYN="N">Copper</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003461" MajorTopicYN="N">Crystallography</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006860" MajorTopicYN="N">Hydrogen Bonding</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="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000648" MajorTopicYN="Y">ultrastructure</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010970" MajorTopicYN="N">Plastocyanin</DescriptorName><QualifierName UI="Q000648" MajorTopicYN="Y">ultrastructure</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012997" MajorTopicYN="N">Solvents</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1990</Year><Month>2</Month><Day>5</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1990</Year><Month>2</Month><Day>5</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1990</Year><Month>2</Month><Day>5</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">2308169</ArticleId><ArticleId IdType="pii">0022-2836(90)90269-R</ArticleId><ArticleId IdType="doi">10.1016/0022-2836(90)90269-R</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Australie</li></country><region><li>Nouvelle-Galles du Sud</li></region><settlement><li>Sydney</li></settlement><orgName><li>Université de Sydney</li></orgName></list><tree><noCountry><name sortKey="Freeman, H C" sort="Freeman, H C" uniqKey="Freeman H" first="H C" last="Freeman">H C Freeman</name><name sortKey="Guss, J M" sort="Guss, J M" uniqKey="Guss J" first="J M" last="Guss">J M Guss</name><name sortKey="Sugimura, Y" sort="Sugimura, Y" uniqKey="Sugimura Y" first="Y" last="Sugimura">Y. Sugimura</name><name sortKey="Yoshizaki, F" sort="Yoshizaki, F" uniqKey="Yoshizaki F" first="F" last="Yoshizaki">F. Yoshizaki</name></noCountry><country name="Australie"><region name="Nouvelle-Galles du Sud"><name sortKey="Collyer, C A" sort="Collyer, C A" uniqKey="Collyer C" first="C A" last="Collyer">C A Collyer</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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