MersV1, PubMed, Corpus, bibRecord, 002071

The peripheral light-harvesting complexes from purple sulfur bacteria have different 'ring' sizes.

Identifieur interne : 002071 ( PubMed/Corpus ); précédent : 002070; suivant : 002072

The peripheral light-harvesting complexes from purple sulfur bacteria have different 'ring' sizes.

Auteurs : Sami Kereïche ; Laurent Bourinet ; Wilko Keegstra ; Ana A. Arteni ; Jean-Marc Verbavatz ; Egbert J. Boekema ; Bruno Robert ; Andrew Gall

Source :

FEBS letters [ 0014-5793 ] ; 2008.

RBID : pubmed:18840433

English descriptors

KwdEn :
- Chromatiaceae (enzymology), Cryoelectron Microscopy, Dimerization, Light-Harvesting Protein Complexes (chemistry), Light-Harvesting Protein Complexes (ultrastructure), Models, Molecular, Particle Size, Protein Conformation.
MESH :
- chemical , chemistry : Light-Harvesting Protein Complexes.
- enzymology : Chromatiaceae.
- chemical , ultrastructure : Light-Harvesting Protein Complexes.
- Cryoelectron Microscopy, Dimerization, Models, Molecular, Particle Size, Protein Conformation.

Abstract

The integral membrane light-harvesting (LH) proteins from purple photosynthetic bacteria form circular oligomers of an elementary unit that is composed of two very hydrophobic polypeptides, termed alpha and beta. These apoprotein dimers are known to associate into closed circular arrays of 8, 9 and 16 alpha/beta-mers. We report the existence of peripheral LH proteins purified from Allochromatium vinosum with two intermediate ring sizes and postulate that one is a 13 alpha/beta-mer. This shows that LH proteins are able to form membrane rings of continuously increasing diameter from 68 to 115A. The presence of these new ring sizes warrants further study, as it will help to further validate the structure-function models of LH proteins currently found in the literature.

DOI: 10.1016/j.febslet.2008.09.050
PubMed: 18840433

Links to Exploration step

pubmed:18840433

Le document en format XML

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<author><name sortKey="Kereiche, Sami" sort="Kereiche, Sami" uniqKey="Kereiche S" first="Sami" last="Kereïche">Sami Kereïche</name>
<affiliation><nlm:affiliation>Department of Biophysical Chemistry, Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands.</nlm:affiliation>
</affiliation>
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<author><name sortKey="Bourinet, Laurent" sort="Bourinet, Laurent" uniqKey="Bourinet L" first="Laurent" last="Bourinet">Laurent Bourinet</name>
</author>
<author><name sortKey="Keegstra, Wilko" sort="Keegstra, Wilko" uniqKey="Keegstra W" first="Wilko" last="Keegstra">Wilko Keegstra</name>
</author>
<author><name sortKey="Arteni, Ana A" sort="Arteni, Ana A" uniqKey="Arteni A" first="Ana A" last="Arteni">Ana A. Arteni</name>
</author>
<author><name sortKey="Verbavatz, Jean Marc" sort="Verbavatz, Jean Marc" uniqKey="Verbavatz J" first="Jean-Marc" last="Verbavatz">Jean-Marc Verbavatz</name>
</author>
<author><name sortKey="Boekema, Egbert J" sort="Boekema, Egbert J" uniqKey="Boekema E" first="Egbert J" last="Boekema">Egbert J. Boekema</name>
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<author><name sortKey="Robert, Bruno" sort="Robert, Bruno" uniqKey="Robert B" first="Bruno" last="Robert">Bruno Robert</name>
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<author><name sortKey="Gall, Andrew" sort="Gall, Andrew" uniqKey="Gall A" first="Andrew" last="Gall">Andrew Gall</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">The peripheral light-harvesting complexes from purple sulfur bacteria have different 'ring' sizes.</title>
<author><name sortKey="Kereiche, Sami" sort="Kereiche, Sami" uniqKey="Kereiche S" first="Sami" last="Kereïche">Sami Kereïche</name>
<affiliation><nlm:affiliation>Department of Biophysical Chemistry, Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands.</nlm:affiliation>
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<author><name sortKey="Bourinet, Laurent" sort="Bourinet, Laurent" uniqKey="Bourinet L" first="Laurent" last="Bourinet">Laurent Bourinet</name>
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<author><name sortKey="Keegstra, Wilko" sort="Keegstra, Wilko" uniqKey="Keegstra W" first="Wilko" last="Keegstra">Wilko Keegstra</name>
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<author><name sortKey="Arteni, Ana A" sort="Arteni, Ana A" uniqKey="Arteni A" first="Ana A" last="Arteni">Ana A. Arteni</name>
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<author><name sortKey="Verbavatz, Jean Marc" sort="Verbavatz, Jean Marc" uniqKey="Verbavatz J" first="Jean-Marc" last="Verbavatz">Jean-Marc Verbavatz</name>
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<author><name sortKey="Boekema, Egbert J" sort="Boekema, Egbert J" uniqKey="Boekema E" first="Egbert J" last="Boekema">Egbert J. Boekema</name>
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<author><name sortKey="Robert, Bruno" sort="Robert, Bruno" uniqKey="Robert B" first="Bruno" last="Robert">Bruno Robert</name>
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<author><name sortKey="Gall, Andrew" sort="Gall, Andrew" uniqKey="Gall A" first="Andrew" last="Gall">Andrew Gall</name>
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<series><title level="j">FEBS letters</title>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Chromatiaceae (enzymology)</term>
<term>Cryoelectron Microscopy</term>
<term>Dimerization</term>
<term>Light-Harvesting Protein Complexes (chemistry)</term>
<term>Light-Harvesting Protein Complexes (ultrastructure)</term>
<term>Models, Molecular</term>
<term>Particle Size</term>
<term>Protein Conformation</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Light-Harvesting Protein Complexes</term>
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<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Chromatiaceae</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="ultrastructure" xml:lang="en"><term>Light-Harvesting Protein Complexes</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Cryoelectron Microscopy</term>
<term>Dimerization</term>
<term>Models, Molecular</term>
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<front><div type="abstract" xml:lang="en">The integral membrane light-harvesting (LH) proteins from purple photosynthetic bacteria form circular oligomers of an elementary unit that is composed of two very hydrophobic polypeptides, termed alpha and beta. These apoprotein dimers are known to associate into closed circular arrays of 8, 9 and 16 alpha/beta-mers. We report the existence of peripheral LH proteins purified from Allochromatium vinosum with two intermediate ring sizes and postulate that one is a 13 alpha/beta-mer. This shows that LH proteins are able to form membrane rings of continuously increasing diameter from 68 to 115A. The presence of these new ring sizes warrants further study, as it will help to further validate the structure-function models of LH proteins currently found in the literature.</div>
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<DateRevised><Year>2008</Year>
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<Month>Oct</Month>
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<Title>FEBS letters</Title>
<ISOAbbreviation>FEBS Lett.</ISOAbbreviation>
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<ArticleTitle>The peripheral light-harvesting complexes from purple sulfur bacteria have different 'ring' sizes.</ArticleTitle>
<Pagination><MedlinePgn>3650-6</MedlinePgn>
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<Abstract><AbstractText>The integral membrane light-harvesting (LH) proteins from purple photosynthetic bacteria form circular oligomers of an elementary unit that is composed of two very hydrophobic polypeptides, termed alpha and beta. These apoprotein dimers are known to associate into closed circular arrays of 8, 9 and 16 alpha/beta-mers. We report the existence of peripheral LH proteins purified from Allochromatium vinosum with two intermediate ring sizes and postulate that one is a 13 alpha/beta-mer. This shows that LH proteins are able to form membrane rings of continuously increasing diameter from 68 to 115A. The presence of these new ring sizes warrants further study, as it will help to further validate the structure-function models of LH proteins currently found in the literature.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kereïche</LastName>
<ForeName>Sami</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>Department of Biophysical Chemistry, Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands.</Affiliation>
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<Language>eng</Language>
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<NameOfSubstance UI="D045342">Light-Harvesting Protein Complexes</NameOfSubstance>
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<MeshHeadingList><MeshHeading><DescriptorName UI="D002841" MajorTopicYN="N">Chromatiaceae</DescriptorName>
<QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName>
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<MeshHeading><DescriptorName UI="D020285" MajorTopicYN="N">Cryoelectron Microscopy</DescriptorName>
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<MeshHeading><DescriptorName UI="D019281" MajorTopicYN="N">Dimerization</DescriptorName>
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<MeshHeading><DescriptorName UI="D045342" MajorTopicYN="N">Light-Harvesting Protein Complexes</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000648" MajorTopicYN="Y">ultrastructure</QualifierName>
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<MeshHeading><DescriptorName UI="D008958" MajorTopicYN="Y">Models, Molecular</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010316" MajorTopicYN="N">Particle Size</DescriptorName>
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<MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName>
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The peripheral light-harvesting complexes from purple sulfur bacteria have different 'ring' sizes.

The peripheral light-harvesting complexes from purple sulfur bacteria have different 'ring' sizes.

Source :

English descriptors

Abstract

Links to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki