Structure of the Cytosolic Part of the Subunit b-Dimer of Escherichia coli F0F1-ATP Synthase
Identifieur interne : 002009 ( Main/Exploration ); précédent : 002008; suivant : 002010Structure of the Cytosolic Part of the Subunit b-Dimer of Escherichia coli F0F1-ATP Synthase
Auteurs : Tassilo Hornung ; Oleg A. Volkov ; Tarek M. A. Zaida ; Sabine Delannoy ; John G. Wise ; Pia D. VogelSource :
- Biophysical Journal [ 0006-3495 ] ; 2008.
Abstract
The structure of the external stalk and its function in the catalytic mechanism of the F0F1-ATP synthase remains one of the important questions in bioenergetics. The external stalk has been proposed to be either a rigid stator that binds F1 or an elastic structural element that transmits energy from the small rotational steps of subunits
Url:
DOI: 10.1529/biophysj.107.121038
PubMed: 18326647
PubMed Central: 2397329
Affiliations:
Links toward previous steps (curation, corpus...)
- to stream Pmc, to step Corpus: 000767
- to stream Pmc, to step Curation: 000766
- to stream Pmc, to step Checkpoint: 001056
- to stream Ncbi, to step Merge: 000804
- to stream Ncbi, to step Curation: 000804
- to stream Ncbi, to step Checkpoint: 000804
- to stream Main, to step Merge: 002063
- to stream Main, to step Curation: 002009
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Structure of the Cytosolic Part of the Subunit <italic>b</italic>
-Dimer of <italic>Escherichia coli</italic>
F<sub>0</sub>
F<sub>1</sub>
-ATP Synthase</title>
<author><name sortKey="Hornung, Tassilo" sort="Hornung, Tassilo" uniqKey="Hornung T" first="Tassilo" last="Hornung">Tassilo Hornung</name>
</author>
<author><name sortKey="Volkov, Oleg A" sort="Volkov, Oleg A" uniqKey="Volkov O" first="Oleg A." last="Volkov">Oleg A. Volkov</name>
</author>
<author><name sortKey="Zaida, Tarek M A" sort="Zaida, Tarek M A" uniqKey="Zaida T" first="Tarek M. A." last="Zaida">Tarek M. A. Zaida</name>
</author>
<author><name sortKey="Delannoy, Sabine" sort="Delannoy, Sabine" uniqKey="Delannoy S" first="Sabine" last="Delannoy">Sabine Delannoy</name>
</author>
<author><name sortKey="Wise, John G" sort="Wise, John G" uniqKey="Wise J" first="John G." last="Wise">John G. Wise</name>
</author>
<author><name sortKey="Vogel, Pia D" sort="Vogel, Pia D" uniqKey="Vogel P" first="Pia D." last="Vogel">Pia D. Vogel</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PMC</idno>
<idno type="pmid">18326647</idno>
<idno type="pmc">2397329</idno>
<idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2397329</idno>
<idno type="RBID">PMC:2397329</idno>
<idno type="doi">10.1529/biophysj.107.121038</idno>
<date when="2008">2008</date>
<idno type="wicri:Area/Pmc/Corpus">000767</idno>
<idno type="wicri:Area/Pmc/Curation">000766</idno>
<idno type="wicri:Area/Pmc/Checkpoint">001056</idno>
<idno type="wicri:Area/Ncbi/Merge">000804</idno>
<idno type="wicri:Area/Ncbi/Curation">000804</idno>
<idno type="wicri:Area/Ncbi/Checkpoint">000804</idno>
<idno type="wicri:doubleKey">0006-3495:2008:Hornung T:structure:of:the</idno>
<idno type="wicri:Area/Main/Merge">002063</idno>
<idno type="wicri:Area/Main/Curation">002009</idno>
<idno type="wicri:Area/Main/Exploration">002009</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Structure of the Cytosolic Part of the Subunit <italic>b</italic>
-Dimer of <italic>Escherichia coli</italic>
F<sub>0</sub>
F<sub>1</sub>
-ATP Synthase</title>
<author><name sortKey="Hornung, Tassilo" sort="Hornung, Tassilo" uniqKey="Hornung T" first="Tassilo" last="Hornung">Tassilo Hornung</name>
</author>
<author><name sortKey="Volkov, Oleg A" sort="Volkov, Oleg A" uniqKey="Volkov O" first="Oleg A." last="Volkov">Oleg A. Volkov</name>
</author>
<author><name sortKey="Zaida, Tarek M A" sort="Zaida, Tarek M A" uniqKey="Zaida T" first="Tarek M. A." last="Zaida">Tarek M. A. Zaida</name>
</author>
<author><name sortKey="Delannoy, Sabine" sort="Delannoy, Sabine" uniqKey="Delannoy S" first="Sabine" last="Delannoy">Sabine Delannoy</name>
</author>
<author><name sortKey="Wise, John G" sort="Wise, John G" uniqKey="Wise J" first="John G." last="Wise">John G. Wise</name>
</author>
<author><name sortKey="Vogel, Pia D" sort="Vogel, Pia D" uniqKey="Vogel P" first="Pia D." last="Vogel">Pia D. Vogel</name>
</author>
</analytic>
<series><title level="j">Biophysical Journal</title>
<idno type="ISSN">0006-3495</idno>
<idno type="eISSN">1542-0086</idno>
<imprint><date when="2008">2008</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass></textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en"><p>The structure of the external stalk and its function in the catalytic mechanism of the F<sub>0</sub>
F<sub>1</sub>
-ATP synthase remains one of the important questions in bioenergetics. The external stalk has been proposed to be either a rigid stator that binds F<sub>1</sub>
or an elastic structural element that transmits energy from the small rotational steps of subunits <italic>c</italic>
to the F<sub>1</sub>
sector during catalysis. We employed proteomics, sequence-based structure prediction, molecular modeling, and electron spin resonance spectroscopy using site-directed spin labeling to understand the structure and interfacial packing of the <italic>Escherichia</italic>
<italic>coli b</italic>
-subunit homodimer external stalk. Comparisons of bacterial, cyanobacterial, and plant <italic>b</italic>
-subunits demonstrated little sequence similarity. Supersecondary structure predictions, however, show that all compared <italic>b</italic>
-sequences have extensive heptad repeats, suggesting that the proteins all are capable of packing as left-handed coiled-coils. Molecular modeling subsequently indicated that <italic>b</italic>
<sub>2</sub>
from the <italic>E. coli</italic>
ATP synthase could pack into stable left-handed coiled-coils. Thirty-eight substitutions to cysteine in soluble <italic>b</italic>
-constructs allowed the introduction of spin labels and the determination of intersubunit distances by ESR. These distances correlated well with molecular modeling results and strongly suggest that the <italic>E. coli</italic>
subunit <italic>b</italic>
-dimer can stably exist as a left-handed coiled-coil.</p>
</div>
</front>
</TEI>
<affiliations><list></list>
<tree><noCountry><name sortKey="Delannoy, Sabine" sort="Delannoy, Sabine" uniqKey="Delannoy S" first="Sabine" last="Delannoy">Sabine Delannoy</name>
<name sortKey="Hornung, Tassilo" sort="Hornung, Tassilo" uniqKey="Hornung T" first="Tassilo" last="Hornung">Tassilo Hornung</name>
<name sortKey="Vogel, Pia D" sort="Vogel, Pia D" uniqKey="Vogel P" first="Pia D." last="Vogel">Pia D. Vogel</name>
<name sortKey="Volkov, Oleg A" sort="Volkov, Oleg A" uniqKey="Volkov O" first="Oleg A." last="Volkov">Oleg A. Volkov</name>
<name sortKey="Wise, John G" sort="Wise, John G" uniqKey="Wise J" first="John G." last="Wise">John G. Wise</name>
<name sortKey="Zaida, Tarek M A" sort="Zaida, Tarek M A" uniqKey="Zaida T" first="Tarek M. A." last="Zaida">Tarek M. A. Zaida</name>
</noCountry>
</tree>
</affiliations>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Bois/explor/OrangerV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 002009 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 002009 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Wicri/Bois |area= OrangerV1 |flux= Main |étape= Exploration |type= RBID |clé= PMC:2397329 |texte= Structure of the Cytosolic Part of the Subunit b-Dimer of Escherichia coli F0F1-ATP Synthase }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:18326647" \ | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \ | NlmPubMed2Wicri -a OrangerV1
![]() | This area was generated with Dilib version V0.6.25. | ![]() |