The structural homology of amicyanin from Thiobacillus versutus to plant plastocyanins.
Identifieur interne : 004C32 ( Main/Exploration ); précédent : 004C31; suivant : 004C33The structural homology of amicyanin from Thiobacillus versutus to plant plastocyanins.
Auteurs : J. Van Beeumen [Belgique] ; S. Van Bun ; G W Canters ; A. Lommen ; C. ChothiaSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 1991.
Descripteurs français
- KwdFr :
- Acides aminés (analyse), Alignement de séquences (MeSH), Chromatographie en phase liquide à haute performance (MeSH), Données de séquences moléculaires (MeSH), Hydrolyse (MeSH), Plantes (métabolisme), Plastocyanine (génétique), Protéines bactériennes (génétique), Pseudomonas (métabolisme), Similitude de séquences d'acides nucléiques (MeSH), Séquence d'acides aminés (MeSH), Thiobacillus (métabolisme).
- MESH :
- analyse : Acides aminés.
- génétique : Plastocyanine, Protéines bactériennes.
- métabolisme : Plantes, Pseudomonas, Thiobacillus.
- Alignement de séquences, Chromatographie en phase liquide à haute performance, Données de séquences moléculaires, Hydrolyse, Similitude de séquences d'acides nucléiques, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Amino Acids (analysis), Bacterial Proteins (genetics), Chromatography, High Pressure Liquid (MeSH), Hydrolysis (MeSH), Molecular Sequence Data (MeSH), Plants (metabolism), Plastocyanin (genetics), Pseudomonas (metabolism), Sequence Alignment (MeSH), Sequence Homology, Nucleic Acid (MeSH), Thiobacillus (metabolism).
- MESH :
- chemical , analysis : Amino Acids.
- chemical , genetics : Bacterial Proteins, Plastocyanin.
- metabolism : Plants, Pseudomonas, Thiobacillus.
- Amino Acid Sequence, Chromatography, High Pressure Liquid, Hydrolysis, Molecular Sequence Data, Sequence Alignment, Sequence Homology, Nucleic Acid.
Abstract
The complete amino acid sequence of the blue copper protein amicyanin of Thiobacillus versutus, induced when the bacterium is grown on methylamine, has been determined as follows: QDKITVTSEKPVAAADVPADAVVVGIEKMKYLTPEVTIKAGETVYWVNGEVMPHNVA FKKGIVGEDAFRGEMMTKDQAYAITFNEAGSYDYFCTPHPFMRGKVIVE. The four copper ligand residues in this 106-residue-containing polypeptide chain are His54, Cys93, His96, and Met99. The Thiobacillus amicyanin is 52% similar to the amicyanin of Pseudomonas AM1, the only other copper protein known with the same spacing between the second histidine ligand and the methionine ligand. T. versutus amicyanin contains no cysteine bridge and is more closely related to the plant copper protein plastocyanin than to the bacterial copper protein azurin. Alignment of the two known amicyanin sequences with the consensus sequence of the plastocyanins and comparison with the known three-dimensional structure of poplar leaves plastocyanin reveals that the bacterial proteins have the same overall structure with two beta-sheets packed face to face. The major structural differences between the amicyanins and the plastocyanins appear to be located in two of the five loops that connect the six identified beta-strands of the amicyanins. The first of these two loops, connecting strands F and G, contains a ligand histidine and must have a different conformation from the same loop in the plastocyanins because it is shorter by two amino acids. Further differences occur in the loop connecting the strands D and E. This loop contains only 17 residues in amicyanin whereas the corresponding loop of plastocyanin contains 25 residues. Despite these differences the amicyanins appear much closer related to the plastocyanins than to the azurins. The present findings demonstrate that the occurrence of blue copper proteins with clearly plastocyanin-like features is not restricted to photosynthetic redox chains.
PubMed: 2002033
Affiliations:
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Van Bun</name></author><author><name sortKey="Canters, G W" sort="Canters, G W" uniqKey="Canters G" first="G W" last="Canters">G W Canters</name></author><author><name sortKey="Lommen, A" sort="Lommen, A" uniqKey="Lommen A" first="A" last="Lommen">A. Lommen</name></author><author><name sortKey="Chothia, C" sort="Chothia, C" uniqKey="Chothia C" first="C" last="Chothia">C. Chothia</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1991">1991</date><idno type="RBID">pubmed:2002033</idno><idno type="pmid">2002033</idno><idno type="wicri:Area/Main/Corpus">004C59</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">004C59</idno><idno type="wicri:Area/Main/Curation">004C59</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">004C59</idno><idno type="wicri:Area/Main/Exploration">004C59</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The structural homology of amicyanin from Thiobacillus versutus to plant plastocyanins.</title><author><name sortKey="Van Beeumen, J" sort="Van Beeumen, J" uniqKey="Van Beeumen J" first="J" last="Van Beeumen">J. Van Beeumen</name><affiliation wicri:level="1"><nlm:affiliation>Laboratory of Microbiology and Microbial Genetics, State University of Ghent, Belgium.</nlm:affiliation><country xml:lang="fr">Belgique</country><wicri:regionArea>Laboratory of Microbiology and Microbial Genetics, State University of Ghent</wicri:regionArea><wicri:noRegion>State University of Ghent</wicri:noRegion></affiliation></author><author><name sortKey="Van Bun, S" sort="Van Bun, S" uniqKey="Van Bun S" first="S" last="Van Bun">S. Van Bun</name></author><author><name sortKey="Canters, G W" sort="Canters, G W" uniqKey="Canters G" first="G W" last="Canters">G W Canters</name></author><author><name sortKey="Lommen, A" sort="Lommen, A" uniqKey="Lommen A" first="A" last="Lommen">A. Lommen</name></author><author><name sortKey="Chothia, C" sort="Chothia, C" uniqKey="Chothia C" first="C" last="Chothia">C. Chothia</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="1991" type="published">1991</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Amino Acids (analysis)</term><term>Bacterial Proteins (genetics)</term><term>Chromatography, High Pressure Liquid (MeSH)</term><term>Hydrolysis (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Plants (metabolism)</term><term>Plastocyanin (genetics)</term><term>Pseudomonas (metabolism)</term><term>Sequence Alignment (MeSH)</term><term>Sequence Homology, Nucleic Acid (MeSH)</term><term>Thiobacillus (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acides aminés (analyse)</term><term>Alignement de séquences (MeSH)</term><term>Chromatographie en phase liquide à haute performance (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Hydrolyse (MeSH)</term><term>Plantes (métabolisme)</term><term>Plastocyanine (génétique)</term><term>Protéines bactériennes (génétique)</term><term>Pseudomonas (métabolisme)</term><term>Similitude de séquences d'acides nucléiques (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Thiobacillus (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Amino Acids</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Bacterial Proteins</term><term>Plastocyanin</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Acides aminés</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Plastocyanine</term><term>Protéines bactériennes</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Plants</term><term>Pseudomonas</term><term>Thiobacillus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Plantes</term><term>Pseudomonas</term><term>Thiobacillus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Chromatography, High Pressure Liquid</term><term>Hydrolysis</term><term>Molecular Sequence Data</term><term>Sequence Alignment</term><term>Sequence Homology, Nucleic Acid</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Chromatographie en phase liquide à haute performance</term><term>Données de séquences moléculaires</term><term>Hydrolyse</term><term>Similitude de séquences d'acides nucléiques</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The complete amino acid sequence of the blue copper protein amicyanin of Thiobacillus versutus, induced when the bacterium is grown on methylamine, has been determined as follows: QDKITVTSEKPVAAADVPADAVVVGIEKMKYLTPEVTIKAGETVYWVNGEVMPHNVA FKKGIVGEDAFRGEMMTKDQAYAITFNEAGSYDYFCTPHPFMRGKVIVE. The four copper ligand residues in this 106-residue-containing polypeptide chain are His54, Cys93, His96, and Met99. The Thiobacillus amicyanin is 52% similar to the amicyanin of Pseudomonas AM1, the only other copper protein known with the same spacing between the second histidine ligand and the methionine ligand. T. versutus amicyanin contains no cysteine bridge and is more closely related to the plant copper protein plastocyanin than to the bacterial copper protein azurin. Alignment of the two known amicyanin sequences with the consensus sequence of the plastocyanins and comparison with the known three-dimensional structure of poplar leaves plastocyanin reveals that the bacterial proteins have the same overall structure with two beta-sheets packed face to face. The major structural differences between the amicyanins and the plastocyanins appear to be located in two of the five loops that connect the six identified beta-strands of the amicyanins. The first of these two loops, connecting strands F and G, contains a ligand histidine and must have a different conformation from the same loop in the plastocyanins because it is shorter by two amino acids. Further differences occur in the loop connecting the strands D and E. This loop contains only 17 residues in amicyanin whereas the corresponding loop of plastocyanin contains 25 residues. Despite these differences the amicyanins appear much closer related to the plastocyanins than to the azurins. The present findings demonstrate that the occurrence of blue copper proteins with clearly plastocyanin-like features is not restricted to photosynthetic redox chains.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">2002033</PMID><DateCompleted><Year>1991</Year><Month>04</Month><Day>17</Day></DateCompleted><DateRevised><Year>2006</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>266</Volume><Issue>8</Issue><PubDate><Year>1991</Year><Month>Mar</Month><Day>15</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>The structural homology of amicyanin from Thiobacillus versutus to plant plastocyanins.</ArticleTitle><Pagination><MedlinePgn>4869-77</MedlinePgn></Pagination><Abstract><AbstractText>The complete amino acid sequence of the blue copper protein amicyanin of Thiobacillus versutus, induced when the bacterium is grown on methylamine, has been determined as follows: QDKITVTSEKPVAAADVPADAVVVGIEKMKYLTPEVTIKAGETVYWVNGEVMPHNVA FKKGIVGEDAFRGEMMTKDQAYAITFNEAGSYDYFCTPHPFMRGKVIVE. The four copper ligand residues in this 106-residue-containing polypeptide chain are His54, Cys93, His96, and Met99. The Thiobacillus amicyanin is 52% similar to the amicyanin of Pseudomonas AM1, the only other copper protein known with the same spacing between the second histidine ligand and the methionine ligand. T. versutus amicyanin contains no cysteine bridge and is more closely related to the plant copper protein plastocyanin than to the bacterial copper protein azurin. Alignment of the two known amicyanin sequences with the consensus sequence of the plastocyanins and comparison with the known three-dimensional structure of poplar leaves plastocyanin reveals that the bacterial proteins have the same overall structure with two beta-sheets packed face to face. The major structural differences between the amicyanins and the plastocyanins appear to be located in two of the five loops that connect the six identified beta-strands of the amicyanins. The first of these two loops, connecting strands F and G, contains a ligand histidine and must have a different conformation from the same loop in the plastocyanins because it is shorter by two amino acids. Further differences occur in the loop connecting the strands D and E. This loop contains only 17 residues in amicyanin whereas the corresponding loop of plastocyanin contains 25 residues. Despite these differences the amicyanins appear much closer related to the plastocyanins than to the azurins. The present findings demonstrate that the occurrence of blue copper proteins with clearly plastocyanin-like features is not restricted to photosynthetic redox chains.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Van Beeumen</LastName><ForeName>J</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Laboratory of Microbiology and Microbial Genetics, State University of Ghent, Belgium.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Van Bun</LastName><ForeName>S</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Canters</LastName><ForeName>G W</ForeName><Initials>GW</Initials></Author><Author ValidYN="Y"><LastName>Lommen</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Chothia</LastName><ForeName>C</ForeName><Initials>C</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="D000596">Amino Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C017079">mauC protein, Methylobacterium extorquens</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="D000596" MajorTopicYN="N">Amino Acids</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001426" MajorTopicYN="N">Bacterial Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002851" MajorTopicYN="N">Chromatography, High Pressure Liquid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006868" MajorTopicYN="N">Hydrolysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010944" MajorTopicYN="N">Plants</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010970" MajorTopicYN="N">Plastocyanin</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011549" MajorTopicYN="N">Pseudomonas</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012689" MajorTopicYN="N">Sequence Homology, Nucleic Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013855" MajorTopicYN="N">Thiobacillus</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1991</Year><Month>3</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1991</Year><Month>3</Month><Day>15</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1991</Year><Month>3</Month><Day>15</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">2002033</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Belgique</li></country></list><tree><noCountry><name sortKey="Canters, G W" sort="Canters, G W" uniqKey="Canters G" first="G W" last="Canters">G W Canters</name><name sortKey="Chothia, C" sort="Chothia, C" uniqKey="Chothia C" first="C" last="Chothia">C. Chothia</name><name sortKey="Lommen, A" sort="Lommen, A" uniqKey="Lommen A" first="A" last="Lommen">A. Lommen</name><name sortKey="Van Bun, S" sort="Van Bun, S" uniqKey="Van Bun S" first="S" last="Van Bun">S. Van Bun</name></noCountry><country name="Belgique"><noRegion><name sortKey="Van Beeumen, J" sort="Van Beeumen, J" uniqKey="Van Beeumen J" first="J" last="Van Beeumen">J. Van Beeumen</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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