Evolution of blue copper proteins.
Identifieur interne : 004D40 ( Main/Exploration ); précédent : 004D39; suivant : 004D41Evolution of blue copper proteins.
Auteurs : L. Rydén [Suède]Source :
- Progress in clinical and biological research [ 0361-7742 ] ; 1988.
Descripteurs français
- KwdFr :
- MESH :
- génétique : Métalloprotéines, Oxidoreductases.
- métabolisme : Cuivre, Métalloprotéines, Oxidoreductases.
- Conformation des protéines, Modèles moléculaires, Protéines bactériennes, Évolution biologique.
English descriptors
- KwdEn :
- MESH :
- chemical , genetics : Metalloproteins, Oxidoreductases.
- chemical , metabolism : Copper, Metalloproteins, Oxidoreductases.
- chemical : Bacterial Proteins.
- Biological Evolution, Models, Molecular, Protein Conformation.
Abstract
The evolutionary relationships of blue copper proteins are reviewed. Five homologous families of small blue proteins are recognized. Despite differences in length their peptide chains can all be accommodated into the eight-stranded fold of plastocyanin with some adjustments at three of the loops and the two termini. The C-termini of the blue oxidases ceruloplasmin and Neurospora laccase also fit into this fold and they are suggested to be homologous to the small blue proteins. The alignment of their amino acid sequences suggest some of the histidines to be binding active site copper. A superposition of the structures of poplar plastocyanin and bovine Cu-Zn superoxide dismutase (SOD) showed that 68 out of 99 alpha-carbons in plastocyanin overlapped with corresponding atoms in SOD with a rms distance of 2.99 A. In addition three of the histidine residues that were proposed to be copper-binding in laccase and ceruloplasmin aligned with ligands to the Cu-Zn pair in a SOD. Thus also SOD might be related to the blue proteins.
PubMed: 3043463
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Rydén</name><affiliation wicri:level="4"><nlm:affiliation>Department of Biochemistry, Uppsala University, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Department of Biochemistry, Uppsala University</wicri:regionArea><placeName><settlement type="city">Uppsala</settlement><region nuts="1">Svealand</region><region nuts="1">East Middle Sweden</region></placeName><orgName type="university">Université d'Uppsala</orgName></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1988">1988</date><idno type="RBID">pubmed:3043463</idno><idno type="pmid">3043463</idno><idno type="wicri:Area/Main/Corpus">004D50</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">004D50</idno><idno type="wicri:Area/Main/Curation">004D50</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">004D50</idno><idno type="wicri:Area/Main/Exploration">004D50</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Evolution of blue copper proteins.</title><author><name sortKey="Ryden, L" sort="Ryden, L" uniqKey="Ryden L" first="L" last="Rydén">L. Rydén</name><affiliation wicri:level="4"><nlm:affiliation>Department of Biochemistry, Uppsala University, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Department of Biochemistry, Uppsala University</wicri:regionArea><placeName><settlement type="city">Uppsala</settlement><region nuts="1">Svealand</region><region nuts="1">East Middle Sweden</region></placeName><orgName type="university">Université d'Uppsala</orgName></affiliation></author></analytic><series><title level="j">Progress in clinical and biological research</title><idno type="ISSN">0361-7742</idno><imprint><date when="1988" type="published">1988</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Bacterial Proteins (MeSH)</term><term>Biological Evolution (MeSH)</term><term>Copper (metabolism)</term><term>Metalloproteins (genetics)</term><term>Metalloproteins (metabolism)</term><term>Models, Molecular (MeSH)</term><term>Oxidoreductases (genetics)</term><term>Oxidoreductases (metabolism)</term><term>Protein Conformation (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Conformation des protéines (MeSH)</term><term>Cuivre (métabolisme)</term><term>Modèles moléculaires (MeSH)</term><term>Métalloprotéines (génétique)</term><term>Métalloprotéines (métabolisme)</term><term>Oxidoreductases (génétique)</term><term>Oxidoreductases (métabolisme)</term><term>Protéines bactériennes (MeSH)</term><term>Évolution biologique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Metalloproteins</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Copper</term><term>Metalloproteins</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Bacterial Proteins</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Métalloprotéines</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cuivre</term><term>Métalloprotéines</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Biological Evolution</term><term>Models, Molecular</term><term>Protein Conformation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Conformation des protéines</term><term>Modèles moléculaires</term><term>Protéines bactériennes</term><term>Évolution biologique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The evolutionary relationships of blue copper proteins are reviewed. Five homologous families of small blue proteins are recognized. Despite differences in length their peptide chains can all be accommodated into the eight-stranded fold of plastocyanin with some adjustments at three of the loops and the two termini. The C-termini of the blue oxidases ceruloplasmin and Neurospora laccase also fit into this fold and they are suggested to be homologous to the small blue proteins. The alignment of their amino acid sequences suggest some of the histidines to be binding active site copper. A superposition of the structures of poplar plastocyanin and bovine Cu-Zn superoxide dismutase (SOD) showed that 68 out of 99 alpha-carbons in plastocyanin overlapped with corresponding atoms in SOD with a rms distance of 2.99 A. In addition three of the histidine residues that were proposed to be copper-binding in laccase and ceruloplasmin aligned with ligands to the Cu-Zn pair in a SOD. Thus also SOD might be related to the blue proteins.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">3043463</PMID><DateCompleted><Year>1988</Year><Month>09</Month><Day>15</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0361-7742</ISSN><JournalIssue CitedMedium="Print"><Volume>274</Volume><PubDate><Year>1988</Year></PubDate></JournalIssue><Title>Progress in clinical and biological research</Title><ISOAbbreviation>Prog Clin Biol Res</ISOAbbreviation></Journal><ArticleTitle>Evolution of blue copper proteins.</ArticleTitle><Pagination><MedlinePgn>349-66</MedlinePgn></Pagination><Abstract><AbstractText>The evolutionary relationships of blue copper proteins are reviewed. Five homologous families of small blue proteins are recognized. Despite differences in length their peptide chains can all be accommodated into the eight-stranded fold of plastocyanin with some adjustments at three of the loops and the two termini. The C-termini of the blue oxidases ceruloplasmin and Neurospora laccase also fit into this fold and they are suggested to be homologous to the small blue proteins. The alignment of their amino acid sequences suggest some of the histidines to be binding active site copper. A superposition of the structures of poplar plastocyanin and bovine Cu-Zn superoxide dismutase (SOD) showed that 68 out of 99 alpha-carbons in plastocyanin overlapped with corresponding atoms in SOD with a rms distance of 2.99 A. In addition three of the histidine residues that were proposed to be copper-binding in laccase and ceruloplasmin aligned with ligands to the Cu-Zn pair in a SOD. Thus also SOD might be related to the blue proteins.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Rydén</LastName><ForeName>L</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, Uppsala University, Sweden.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Prog Clin Biol Res</MedlineTA><NlmUniqueID>7605701</NlmUniqueID><ISSNLinking>0361-7742</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008667">Metalloproteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C017079">mauC protein, Methylobacterium extorquens</NameOfSubstance></Chemical><Chemical><RegistryNumber>789U1901C5</RegistryNumber><NameOfSubstance UI="D003300">Copper</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CitationSubset>S</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001426" MajorTopicYN="Y">Bacterial Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005075" MajorTopicYN="Y">Biological Evolution</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003300" MajorTopicYN="N">Copper</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008667" MajorTopicYN="N">Metalloproteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading></MeshHeadingList><NumberOfReferences>34</NumberOfReferences><OtherID Source="NASA">88303947</OtherID></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1988</Year><Month>1</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1988</Year><Month>1</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1988</Year><Month>1</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">3043463</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Suède</li></country><region><li>East Middle Sweden</li><li>Svealand</li></region><settlement><li>Uppsala</li></settlement><orgName><li>Université d'Uppsala</li></orgName></list><tree><country name="Suède"><region name="Svealand"><name sortKey="Ryden, L" sort="Ryden, L" uniqKey="Ryden L" first="L" last="Rydén">L. 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