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Structure of the Cytosolic Part of the Subunit b-Dimer of Escherichia coli F0F1-ATP Synthase

Identifieur interne : 001056 ( Pmc/Checkpoint ); précédent : 001055; suivant : 001057

Structure 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. Vogel

Source :

RBID : PMC:2397329

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 c to the F1 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 Escherichia coli b-subunit homodimer external stalk. Comparisons of bacterial, cyanobacterial, and plant b-subunits demonstrated little sequence similarity. Supersecondary structure predictions, however, show that all compared b-sequences have extensive heptad repeats, suggesting that the proteins all are capable of packing as left-handed coiled-coils. Molecular modeling subsequently indicated that b2 from the E. coli ATP synthase could pack into stable left-handed coiled-coils. Thirty-eight substitutions to cysteine in soluble b-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 E. coli subunit b-dimer can stably exist as a left-handed coiled-coil.


Url:
DOI: 10.1529/biophysj.107.121038
PubMed: 18326647
PubMed Central: 2397329


Affiliations:

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PMC:2397329

Le document en format XML

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<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>
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<idno type="pmid">18326647</idno>
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<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>
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<name sortKey="Volkov, Oleg A" sort="Volkov, Oleg A" uniqKey="Volkov O" first="Oleg A." last="Volkov">Oleg A. Volkov</name>
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<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>
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<author>
<name sortKey="Delannoy, Sabine" sort="Delannoy, Sabine" uniqKey="Delannoy S" first="Sabine" last="Delannoy">Sabine Delannoy</name>
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<author>
<name sortKey="Wise, John G" sort="Wise, John G" uniqKey="Wise J" first="John G." last="Wise">John G. Wise</name>
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<author>
<name sortKey="Vogel, Pia D" sort="Vogel, Pia D" uniqKey="Vogel P" first="Pia D." last="Vogel">Pia D. Vogel</name>
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<series>
<title level="j">Biophysical Journal</title>
<idno type="ISSN">0006-3495</idno>
<idno type="eISSN">1542-0086</idno>
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<date when="2008">2008</date>
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<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>
<pmc article-type="research-article">
<pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front>
<journal-meta>
<journal-id journal-id-type="nlm-ta">Biophys J</journal-id>
<journal-id journal-id-type="publisher-id">biophysj</journal-id>
<journal-title>Biophysical Journal</journal-title>
<issn pub-type="ppub">0006-3495</issn>
<issn pub-type="epub">1542-0086</issn>
<publisher>
<publisher-name>The Biophysical Society</publisher-name>
</publisher>
</journal-meta>
<article-meta>
<article-id pub-id-type="pmid">18326647</article-id>
<article-id pub-id-type="pmc">2397329</article-id>
<article-id pub-id-type="publisher-id">121038</article-id>
<article-id pub-id-type="doi">10.1529/biophysj.107.121038</article-id>
<article-categories>
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<subject>Other</subject>
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</article-categories>
<title-group>
<article-title>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</article-title>
</title-group>
<contrib-group>
<contrib contrib-type="author">
<name>
<surname>Hornung</surname>
<given-names>Tassilo</given-names>
</name>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Volkov</surname>
<given-names>Oleg A.</given-names>
</name>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Zaida</surname>
<given-names>Tarek M. A.</given-names>
</name>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Delannoy</surname>
<given-names>Sabine</given-names>
</name>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Wise</surname>
<given-names>John G.</given-names>
</name>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Vogel</surname>
<given-names>Pia D.</given-names>
</name>
</contrib>
</contrib-group>
<aff id="N0x1c5c9c0N0x4313398">Department of Biological Sciences, Southern Methodist University, Dallas, Texas</aff>
<author-notes>
<fn>
<p>Address reprint requests to Pia D. Vogel, Dept. of Biological Sciences, Southern Methodist University, Dallas, TX, Tel.: 214-768-1790; Fax: 214-768-3955; E-mail:
<email>pvogel@smu.edu</email>
.</p>
</fn>
</author-notes>
<pub-date pub-type="ppub">
<day>15</day>
<month>6</month>
<year>2008</year>
</pub-date>
<pub-date pub-type="epub">
<day>7</day>
<month>3</month>
<year>2008</year>
</pub-date>
<volume>94</volume>
<issue>12</issue>
<fpage>5053</fpage>
<lpage>5064</lpage>
<history>
<date date-type="received">
<day>30</day>
<month>8</month>
<year>2007</year>
</date>
<date date-type="accepted">
<day>29</day>
<month>1</month>
<year>2008</year>
</date>
</history>
<permissions>
<copyright-statement>Copyright © 2008, Biophysical Society</copyright-statement>
</permissions>
<abstract>
<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>
</abstract>
</article-meta>
<notes>
<fn-group>
<fn>
<p>Tassilo Hornung's present address is Biomedicine and Biotechnology, School of Life Sciences, Arizona State University, Tempe, AZ.</p>
</fn>
<fn>
<p>Sabine Delannoy's present address is Agence Française de Sécurité Sanitaire des Aliments, Maisons-Alfort, France.</p>
</fn>
<fn>
<p>Editor: David D. Thomas.</p>
</fn>
</fn-group>
</notes>
</front>
</pmc>
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<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>
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