Structure and Function of the Catalytic Domain of the Dihydrolipoyl Acetyltransferase Component in Escherichia coli Pyruvate Dehydrogenase Complex*
Identifieur interne : 000984 ( Pmc/Curation ); précédent : 000983; suivant : 000985Structure and Function of the Catalytic Domain of the Dihydrolipoyl Acetyltransferase Component in Escherichia coli Pyruvate Dehydrogenase Complex*
Auteurs : Junjie Wang ; Natalia S. Nemeria ; Krishnamoorthy Chandrasekhar ; Sowmini Kumaran ; Palaniappa Arjunan ; Shelley Reynolds ; Guillermo Calero ; Roman Brukh ; Lazaros Kakalis ; William Furey ; Frank JordanSource :
- The Journal of Biological Chemistry [ 0021-9258 ] ; 2014.
Abstract
Url:
DOI: 10.1074/jbc.M113.544080
PubMed: 24742683
PubMed Central: 4140881
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Structure and Function of the Catalytic Domain of the Dihydrolipoyl Acetyltransferase Component in <italic>Escherichia coli</italic>
Pyruvate Dehydrogenase Complex<xref ref-type="fn" rid="FN1">*</xref>
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</sup>
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</title>
<author><name sortKey="Wang, Junjie" sort="Wang, Junjie" uniqKey="Wang J" first="Junjie" last="Wang">Junjie Wang</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Nemeria, Natalia S" sort="Nemeria, Natalia S" uniqKey="Nemeria N" first="Natalia S." last="Nemeria">Natalia S. Nemeria</name>
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<author><name sortKey="Chandrasekhar, Krishnamoorthy" sort="Chandrasekhar, Krishnamoorthy" uniqKey="Chandrasekhar K" first="Krishnamoorthy" last="Chandrasekhar">Krishnamoorthy Chandrasekhar</name>
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</affiliation>
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<author><name sortKey="Kumaran, Sowmini" sort="Kumaran, Sowmini" uniqKey="Kumaran S" first="Sowmini" last="Kumaran">Sowmini Kumaran</name>
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<author><name sortKey="Arjunan, Palaniappa" sort="Arjunan, Palaniappa" uniqKey="Arjunan P" first="Palaniappa" last="Arjunan">Palaniappa Arjunan</name>
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<author><name sortKey="Reynolds, Shelley" sort="Reynolds, Shelley" uniqKey="Reynolds S" first="Shelley" last="Reynolds">Shelley Reynolds</name>
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<author><name sortKey="Calero, Guillermo" sort="Calero, Guillermo" uniqKey="Calero G" first="Guillermo" last="Calero">Guillermo Calero</name>
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<author><name sortKey="Brukh, Roman" sort="Brukh, Roman" uniqKey="Brukh R" first="Roman" last="Brukh">Roman Brukh</name>
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<author><name sortKey="Kakalis, Lazaros" sort="Kakalis, Lazaros" uniqKey="Kakalis L" first="Lazaros" last="Kakalis">Lazaros Kakalis</name>
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</affiliation>
</author>
<author><name sortKey="Furey, William" sort="Furey, William" uniqKey="Furey W" first="William" last="Furey">William Furey</name>
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</affiliation>
<affiliation><nlm:aff id="aff3"></nlm:aff>
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<author><name sortKey="Jordan, Frank" sort="Jordan, Frank" uniqKey="Jordan F" first="Frank" last="Jordan">Frank Jordan</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Structure and Function of the Catalytic Domain of the Dihydrolipoyl Acetyltransferase Component in <italic>Escherichia coli</italic>
Pyruvate Dehydrogenase Complex<xref ref-type="fn" rid="FN1">*</xref>
<xref ref-type="fn" rid="FN2"><sup><inline-graphic xlink:href="sbox.jpg"></inline-graphic>
</sup>
</xref>
</title>
<author><name sortKey="Wang, Junjie" sort="Wang, Junjie" uniqKey="Wang J" first="Junjie" last="Wang">Junjie Wang</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Nemeria, Natalia S" sort="Nemeria, Natalia S" uniqKey="Nemeria N" first="Natalia S." last="Nemeria">Natalia S. Nemeria</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Chandrasekhar, Krishnamoorthy" sort="Chandrasekhar, Krishnamoorthy" uniqKey="Chandrasekhar K" first="Krishnamoorthy" last="Chandrasekhar">Krishnamoorthy Chandrasekhar</name>
<affiliation><nlm:aff id="aff2"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Kumaran, Sowmini" sort="Kumaran, Sowmini" uniqKey="Kumaran S" first="Sowmini" last="Kumaran">Sowmini Kumaran</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Arjunan, Palaniappa" sort="Arjunan, Palaniappa" uniqKey="Arjunan P" first="Palaniappa" last="Arjunan">Palaniappa Arjunan</name>
<affiliation><nlm:aff id="aff2"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Reynolds, Shelley" sort="Reynolds, Shelley" uniqKey="Reynolds S" first="Shelley" last="Reynolds">Shelley Reynolds</name>
<affiliation><nlm:aff id="aff4"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Calero, Guillermo" sort="Calero, Guillermo" uniqKey="Calero G" first="Guillermo" last="Calero">Guillermo Calero</name>
<affiliation><nlm:aff id="aff4"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Brukh, Roman" sort="Brukh, Roman" uniqKey="Brukh R" first="Roman" last="Brukh">Roman Brukh</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Kakalis, Lazaros" sort="Kakalis, Lazaros" uniqKey="Kakalis L" first="Lazaros" last="Kakalis">Lazaros Kakalis</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Furey, William" sort="Furey, William" uniqKey="Furey W" first="William" last="Furey">William Furey</name>
<affiliation><nlm:aff id="aff2"></nlm:aff>
</affiliation>
<affiliation><nlm:aff id="aff3"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Jordan, Frank" sort="Jordan, Frank" uniqKey="Jordan F" first="Frank" last="Jordan">Frank Jordan</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
</analytic>
<series><title level="j">The Journal of Biological Chemistry</title>
<idno type="ISSN">0021-9258</idno>
<idno type="eISSN">1083-351X</idno>
<imprint><date when="2014">2014</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
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<front><div type="abstract" xml:lang="en"><p><bold>Background:</bold>
The <italic>E. coli</italic>
pyruvate dehydrogenase complex catalyzes conversion of pyruvate to acetyl-CoA and comprises E1p, E2p, and E3 components.</p>
<p><bold>Results:</bold>
The structure of the E2 core domain was solved and shown to efficiently catalyze acetyl transfer between domains.</p>
<p><bold>Conclusion:</bold>
Mass spectrometry revealed hitherto unrecognized domain-induced interactions between E1 and E2 core domain.</p>
<p><bold>Significance:</bold>
A multifaceted approach is required to understand communication between intact multidomain components.</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">J Biol Chem</journal-id>
<journal-id journal-id-type="iso-abbrev">J. Biol. Chem</journal-id>
<journal-id journal-id-type="hwp">jbc</journal-id>
<journal-id journal-id-type="pmc">jbc</journal-id>
<journal-id journal-id-type="publisher-id">JBC</journal-id>
<journal-title-group><journal-title>The Journal of Biological Chemistry</journal-title>
</journal-title-group>
<issn pub-type="ppub">0021-9258</issn>
<issn pub-type="epub">1083-351X</issn>
<publisher><publisher-name>American Society for Biochemistry and Molecular Biology</publisher-name>
<publisher-loc>9650 Rockville Pike, Bethesda, MD 20814, U.S.A.</publisher-loc>
</publisher>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">24742683</article-id>
<article-id pub-id-type="pmc">4140881</article-id>
<article-id pub-id-type="publisher-id">M113.544080</article-id>
<article-id pub-id-type="doi">10.1074/jbc.M113.544080</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Enzymology</subject>
</subj-group>
</article-categories>
<title-group><article-title>Structure and Function of the Catalytic Domain of the Dihydrolipoyl Acetyltransferase Component in <italic>Escherichia coli</italic>
Pyruvate Dehydrogenase Complex<xref ref-type="fn" rid="FN1">*</xref>
<xref ref-type="fn" rid="FN2"><sup><inline-graphic xlink:href="sbox.jpg"></inline-graphic>
</sup>
</xref>
</article-title>
<alt-title alt-title-type="short">Roles of E2 Domains in Pyruvate Dehydrogenase Complex</alt-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Wang</surname>
<given-names>Junjie</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>‡</sup>
</xref>
<xref ref-type="author-notes" rid="FN3"><sup>1</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Nemeria</surname>
<given-names>Natalia S.</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>‡</sup>
</xref>
<xref ref-type="author-notes" rid="FN3"><sup>1</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Chandrasekhar</surname>
<given-names>Krishnamoorthy</given-names>
</name>
<xref ref-type="aff" rid="aff2"><sup>§</sup>
</xref>
<xref ref-type="author-notes" rid="FN3"><sup>1</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Kumaran</surname>
<given-names>Sowmini</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>‡</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Arjunan</surname>
<given-names>Palaniappa</given-names>
</name>
<xref ref-type="aff" rid="aff2"><sup>§</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Reynolds</surname>
<given-names>Shelley</given-names>
</name>
<xref ref-type="aff" rid="aff4"><sup>¶</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Calero</surname>
<given-names>Guillermo</given-names>
</name>
<xref ref-type="aff" rid="aff4"><sup>¶</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Brukh</surname>
<given-names>Roman</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>‡</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Kakalis</surname>
<given-names>Lazaros</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>‡</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Furey</surname>
<given-names>William</given-names>
</name>
<xref ref-type="aff" rid="aff2"><sup>§</sup>
</xref>
<xref ref-type="aff" rid="aff3"><sup>‖</sup>
</xref>
<xref ref-type="corresp" rid="cor1"><sup>2</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Jordan</surname>
<given-names>Frank</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>‡</sup>
</xref>
<xref ref-type="corresp" rid="cor2"><sup>3</sup>
</xref>
</contrib>
<aff id="aff1">From the<label>‡</label>
Department of Chemistry, Rutgers University, Newark, New Jersey 07102,</aff>
<aff id="aff2">the<label>§</label>
Department of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261,</aff>
<aff id="aff3">the<label>‖</label>
Veterans Affairs Medical Center, Pittsburgh, Pennsylvania 15240, and</aff>
<aff id="aff4">the<label>¶</label>
Department of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261</aff>
</contrib-group>
<author-notes><corresp id="cor1"><label>2</label>
To whom correspondence may be addressed: <addr-line>Dept. of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15261.</addr-line>
Tel.: <phone>412-607-3106</phone>
; E-mail: <email>fureyw@pitt.edu</email>
.</corresp>
<corresp id="cor2"><label>3</label>
To whom correspondence may be addressed. Tel.: <phone>973-353-5470</phone>
; E-mail: <email>frjordan@rutgers.edu</email>
.</corresp>
<fn fn-type="equal" id="FN3"><label>1</label>
<p>These authors contributed equally to this work.</p>
</fn>
</author-notes>
<pub-date pub-type="ppub"><day>30</day>
<month>5</month>
<year>2014</year>
</pub-date>
<pub-date pub-type="epub"><day>17</day>
<month>4</month>
<year>2014</year>
</pub-date>
<volume>289</volume>
<issue>22</issue>
<fpage>15215</fpage>
<lpage>15230</lpage>
<history><date date-type="received"><day>21</day>
<month>12</month>
<year>2013</year>
</date>
<date date-type="rev-recd"><day>16</day>
<month>4</month>
<year>2014</year>
</date>
</history>
<permissions><copyright-statement>© 2014 by The American Society for Biochemistry and Molecular Biology, Inc.</copyright-statement>
<copyright-year>2014</copyright-year>
</permissions>
<self-uri xlink:title="pdf" xlink:type="simple" xlink:href="zbc02214015215.pdf"></self-uri>
<abstract abstract-type="teaser"><p><bold>Background:</bold>
The <italic>E. coli</italic>
pyruvate dehydrogenase complex catalyzes conversion of pyruvate to acetyl-CoA and comprises E1p, E2p, and E3 components.</p>
<p><bold>Results:</bold>
The structure of the E2 core domain was solved and shown to efficiently catalyze acetyl transfer between domains.</p>
<p><bold>Conclusion:</bold>
Mass spectrometry revealed hitherto unrecognized domain-induced interactions between E1 and E2 core domain.</p>
<p><bold>Significance:</bold>
A multifaceted approach is required to understand communication between intact multidomain components.</p>
</abstract>
<abstract><p>The <italic>Escherichia coli</italic>
pyruvate dehydrogenase complex (PDHc) catalyzing conversion of pyruvate to acetyl-CoA comprises three components: E1p, E2p, and E3. The E2p is the five-domain core component, consisting of three tandem lipoyl domains (LDs), a peripheral subunit binding domain (PSBD), and a catalytic domain (E2pCD). Herein are reported the following. 1) The x-ray structure of E2pCD revealed both intra- and intertrimer interactions, similar to those reported for other E2pCDs. 2) Reconstitution of recombinant LD and E2pCD with E1p and E3p into PDHc could maintain at least 6.4% activity (NADH production), confirming the functional competence of the E2pCD and active center coupling among E1p, LD, E2pCD, and E3 even in the absence of PSBD and of a covalent link between domains within E2p. 3) Direct acetyl transfer between LD and coenzyme A catalyzed by E2pCD was observed with a rate constant of 199 s<sup>−1</sup>
, comparable with the rate of NADH production in the PDHc reaction. Hence, neither reductive acetylation of E2p nor acetyl transfer within E2p is rate-limiting. 4) An unprecedented finding is that although no interaction could be detected between E1p and E2pCD by itself, a domain-induced interaction was identified on E1p active centers upon assembly with E2p and C-terminally truncated E2p proteins by hydrogen/deuterium exchange mass spectrometry. The inclusion of each additional domain of E2p strengthened the interaction with E1p, and the interaction was strongest with intact E2p. E2p domain-induced changes at the E1p active site were also manifested by the appearance of a circular dichroism band characteristic of the canonical 4′-aminopyrimidine tautomer of bound thiamin diphosphate (AP).</p>
</abstract>
<kwd-group><kwd>Carbohydrate Metabolism</kwd>
<kwd>Enzyme Catalysis</kwd>
<kwd>Mass Spectrometry (MS)</kwd>
<kwd>Nuclear Magnetic Resonance (NMR)</kwd>
<kwd>Pyruvate Dehydrogenase Complex (PDC)</kwd>
<kwd>X-ray Crystallography</kwd>
<kwd>HD Exchange</kwd>
</kwd-group>
<funding-group><award-group><funding-source id="CS100">National Institutes of Health</funding-source>
<award-id rid="CS100">GM061791</award-id>
<award-id rid="CS100">GM050380</award-id>
</award-group>
</funding-group>
</article-meta>
</front>
</pmc>
</record>
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