1H NMR studies of plastocyanin from Scenedesmus obliquus: complete sequence-specific assignment, secondary structure analysis, and global fold.
Identifieur interne : 004D50 ( Main/Exploration ); précédent : 004D49; suivant : 004D511H NMR studies of plastocyanin from Scenedesmus obliquus: complete sequence-specific assignment, secondary structure analysis, and global fold.
Auteurs : J M Moore [États-Unis] ; W J Chazin ; R. Powls ; P E WrightSource :
- Biochemistry [ 0006-2960 ] ; 1988.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical : Plant Proteins, Plastocyanin, Spin Labels.
- analysis : Chlorophyta.
- Amino Acid Sequence, Magnetic Resonance Spectroscopy, Molecular Sequence Data, Protein Conformation.
Abstract
Two-dimensional 1H NMR methods have been used to make sequence-specific resonance assignments for the 97 amino acid residues of the plastocyanin from the green alga Scenedesmus obliquus. Assignments were obtained for all backbone protons and the majority of the side-chain protons. Spin system identification relied heavily on the observation of relayed connectivities to the backbone amide proton. Sequence-specific assignments were made by using the sequential assignment procedure. During this process, an extra valine residue was identified that had not been detected in the original amino acid sequence. Elements of regular secondary structure were identified from characteristic NOE connectivities between backbone protons, 3JHN alpha coupling constant values, and the observation of slowly exchanging amide protons. The protein in solution contains eight beta-strands, one short segment of helix, five reverse turns, and five loops. The beta-strands may be arranged into two beta-sheets on the basis of extensive cross-strand NOE connectivities. The chain-folding topology determined from the NMR experiments is that of a Greek key beta-barrel and is similar to that observed for French bean plastocyanin in solution and poplar plastocyanin in the crystalline state. While the overall structures are similar, several differences in local structure between the S. obliquus and higher plant plastocyanins have been identified.
DOI: 10.1021/bi00420a033
PubMed: 3207712
Affiliations:
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Powls</name></author><author><name sortKey="Wright, P E" sort="Wright, P E" uniqKey="Wright P" first="P E" last="Wright">P E Wright</name></author></analytic><series><title level="j">Biochemistry</title><idno type="ISSN">0006-2960</idno><imprint><date when="1988" type="published">1988</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Chlorophyta (analysis)</term><term>Magnetic Resonance Spectroscopy (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Plant Proteins (MeSH)</term><term>Plastocyanin (MeSH)</term><term>Protein Conformation (MeSH)</term><term>Spin Labels (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Chlorophyta (analyse)</term><term>Conformation des protéines (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Marqueurs de spin (MeSH)</term><term>Plastocyanine (MeSH)</term><term>Protéines végétales (MeSH)</term><term>Spectroscopie par résonance magnétique (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Plant Proteins</term><term>Plastocyanin</term><term>Spin Labels</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Chlorophyta</term></keywords><keywords scheme="MESH" qualifier="analysis" xml:lang="en"><term>Chlorophyta</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Magnetic Resonance Spectroscopy</term><term>Molecular Sequence Data</term><term>Protein Conformation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Conformation des protéines</term><term>Données de séquences moléculaires</term><term>Marqueurs de spin</term><term>Plastocyanine</term><term>Protéines végétales</term><term>Spectroscopie par résonance magnétique</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Two-dimensional 1H NMR methods have been used to make sequence-specific resonance assignments for the 97 amino acid residues of the plastocyanin from the green alga Scenedesmus obliquus. Assignments were obtained for all backbone protons and the majority of the side-chain protons. Spin system identification relied heavily on the observation of relayed connectivities to the backbone amide proton. Sequence-specific assignments were made by using the sequential assignment procedure. During this process, an extra valine residue was identified that had not been detected in the original amino acid sequence. Elements of regular secondary structure were identified from characteristic NOE connectivities between backbone protons, 3JHN alpha coupling constant values, and the observation of slowly exchanging amide protons. The protein in solution contains eight beta-strands, one short segment of helix, five reverse turns, and five loops. The beta-strands may be arranged into two beta-sheets on the basis of extensive cross-strand NOE connectivities. The chain-folding topology determined from the NMR experiments is that of a Greek key beta-barrel and is similar to that observed for French bean plastocyanin in solution and poplar plastocyanin in the crystalline state. While the overall structures are similar, several differences in local structure between the S. obliquus and higher plant plastocyanins have been identified.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">3207712</PMID><DateCompleted><Year>1989</Year><Month>02</Month><Day>23</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>13</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-2960</ISSN><JournalIssue CitedMedium="Print"><Volume>27</Volume><Issue>20</Issue><PubDate><Year>1988</Year><Month>Oct</Month><Day>04</Day></PubDate></JournalIssue><Title>Biochemistry</Title><ISOAbbreviation>Biochemistry</ISOAbbreviation></Journal><ArticleTitle>1H NMR studies of plastocyanin from Scenedesmus obliquus: complete sequence-specific assignment, secondary structure analysis, and global fold.</ArticleTitle><Pagination><MedlinePgn>7806-16</MedlinePgn></Pagination><Abstract><AbstractText>Two-dimensional 1H NMR methods have been used to make sequence-specific resonance assignments for the 97 amino acid residues of the plastocyanin from the green alga Scenedesmus obliquus. Assignments were obtained for all backbone protons and the majority of the side-chain protons. Spin system identification relied heavily on the observation of relayed connectivities to the backbone amide proton. Sequence-specific assignments were made by using the sequential assignment procedure. During this process, an extra valine residue was identified that had not been detected in the original amino acid sequence. Elements of regular secondary structure were identified from characteristic NOE connectivities between backbone protons, 3JHN alpha coupling constant values, and the observation of slowly exchanging amide protons. The protein in solution contains eight beta-strands, one short segment of helix, five reverse turns, and five loops. The beta-strands may be arranged into two beta-sheets on the basis of extensive cross-strand NOE connectivities. The chain-folding topology determined from the NMR experiments is that of a Greek key beta-barrel and is similar to that observed for French bean plastocyanin in solution and poplar plastocyanin in the crystalline state. While the overall structures are similar, several differences in local structure between the S. obliquus and higher plant plastocyanins have been identified.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Moore</LastName><ForeName>J M</ForeName><Initials>JM</Initials><AffiliationInfo><Affiliation>Department of Molecular Biology, Research Institute of Scripps Clinic, La Jolla, California 92037.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chazin</LastName><ForeName>W J</ForeName><Initials>WJ</Initials></Author><Author ValidYN="Y"><LastName>Powls</LastName><ForeName>R</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Wright</LastName><ForeName>P E</ForeName><Initials>PE</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>GM36643</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochemistry</MedlineTA><NlmUniqueID>0370623</NlmUniqueID><ISSNLinking>0006-2960</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013113">Spin Labels</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><QualifierName UI="Q000032" MajorTopicYN="Y">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009682" MajorTopicYN="N">Magnetic Resonance Spectroscopy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="Y">Plant Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010970" MajorTopicYN="Y">Plastocyanin</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013113" MajorTopicYN="N">Spin Labels</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1988</Year><Month>10</Month><Day>4</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1988</Year><Month>10</Month><Day>4</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1988</Year><Month>10</Month><Day>4</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">3207712</ArticleId><ArticleId IdType="doi">10.1021/bi00420a033</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Californie</li></region></list><tree><noCountry><name sortKey="Chazin, W J" sort="Chazin, W J" uniqKey="Chazin W" first="W J" last="Chazin">W J Chazin</name><name sortKey="Powls, R" sort="Powls, R" uniqKey="Powls R" first="R" last="Powls">R. Powls</name><name sortKey="Wright, P E" sort="Wright, P E" uniqKey="Wright P" first="P E" last="Wright">P E Wright</name></noCountry><country name="États-Unis"><region name="Californie"><name sortKey="Moore, J M" sort="Moore, J M" uniqKey="Moore J" first="J M" last="Moore">J M Moore</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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