Structure and Function of the Catalytic Domain of the Dihydrolipoyl Acetyltransferase Component in Escherichia coli Pyruvate Dehydrogenase Complex*
Identifieur interne : 000498 ( Pmc/Checkpoint ); précédent : 000497; suivant : 000499Structure 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
Affiliations:
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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><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></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">24742683</idno><idno type="pmc">4140881</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4140881</idno><idno type="RBID">PMC:4140881</idno><idno type="doi">10.1074/jbc.M113.544080</idno><date when="2014">2014</date><idno type="wicri:Area/Pmc/Corpus">000A09</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000A09</idno><idno type="wicri:Area/Pmc/Curation">000984</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000984</idno><idno type="wicri:Area/Pmc/Checkpoint">000498</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">000498</idno></publicationStmt><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></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><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><affiliations><list></list><tree><noCountry><name sortKey="Arjunan, Palaniappa" sort="Arjunan, Palaniappa" uniqKey="Arjunan P" first="Palaniappa" last="Arjunan">Palaniappa Arjunan</name><name sortKey="Brukh, Roman" sort="Brukh, Roman" uniqKey="Brukh R" first="Roman" last="Brukh">Roman Brukh</name><name sortKey="Calero, Guillermo" sort="Calero, Guillermo" uniqKey="Calero G" first="Guillermo" last="Calero">Guillermo Calero</name><name sortKey="Chandrasekhar, Krishnamoorthy" sort="Chandrasekhar, Krishnamoorthy" uniqKey="Chandrasekhar K" first="Krishnamoorthy" last="Chandrasekhar">Krishnamoorthy Chandrasekhar</name><name sortKey="Furey, William" sort="Furey, William" uniqKey="Furey W" first="William" last="Furey">William Furey</name><name sortKey="Jordan, Frank" sort="Jordan, Frank" uniqKey="Jordan F" first="Frank" last="Jordan">Frank Jordan</name><name sortKey="Kakalis, Lazaros" sort="Kakalis, Lazaros" uniqKey="Kakalis L" first="Lazaros" last="Kakalis">Lazaros Kakalis</name><name sortKey="Kumaran, Sowmini" sort="Kumaran, Sowmini" uniqKey="Kumaran S" first="Sowmini" last="Kumaran">Sowmini Kumaran</name><name sortKey="Nemeria, Natalia S" sort="Nemeria, Natalia S" uniqKey="Nemeria N" first="Natalia S." last="Nemeria">Natalia S. Nemeria</name><name sortKey="Reynolds, Shelley" sort="Reynolds, Shelley" uniqKey="Reynolds S" first="Shelley" last="Reynolds">Shelley Reynolds</name><name sortKey="Wang, Junjie" sort="Wang, Junjie" uniqKey="Wang J" first="Junjie" last="Wang">Junjie Wang</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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