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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Structure and function of an insect α-carboxylesterase (α<italic>Esterase</italic>7) associated with insecticide resistance</title><author><name sortKey="Jackson, Colin J" sort="Jackson, Colin J" uniqKey="Jackson C" first="Colin J." last="Jackson">Colin J. Jackson</name><affiliation><nlm:aff id="aff1">Research School of Chemistry,<institution>Australian National University</institution>, Canberra, ACT 0200,<country>Australia</country>;</nlm:aff></affiliation><affiliation><nlm:aff wicri:cut="; and" id="aff2"><institution>Institut de Biologie Structurale</institution>, Commissariat a l'Energie Atomique, F-38027 Grenoble,<country>France</country></nlm:aff></affiliation></author><author><name sortKey="Liu, Jian Wei" sort="Liu, Jian Wei" uniqKey="Liu J" first="Jian-Wei" last="Liu">Jian-Wei Liu</name><affiliation><nlm:aff id="aff3"><institution>Commonwealth Scientific and Industrial Research Organization (Australia) Ecosystems Science</institution>, Canberra, ACT 0200,<country>Australia</country></nlm:aff></affiliation></author><author><name sortKey="Carr, Paul D" sort="Carr, Paul D" uniqKey="Carr P" first="Paul D." last="Carr">Paul D. Carr</name><affiliation><nlm:aff id="aff1">Research School of Chemistry,<institution>Australian National University</institution>, Canberra, ACT 0200,<country>Australia</country>;</nlm:aff></affiliation></author><author><name sortKey="Younus, Faisal" sort="Younus, Faisal" uniqKey="Younus F" first="Faisal" last="Younus">Faisal Younus</name><affiliation><nlm:aff id="aff3"><institution>Commonwealth Scientific and Industrial Research Organization (Australia) Ecosystems Science</institution>, Canberra, ACT 0200,<country>Australia</country></nlm:aff></affiliation></author><author><name sortKey="Coppin, Chris" sort="Coppin, Chris" uniqKey="Coppin C" first="Chris" last="Coppin">Chris Coppin</name><affiliation><nlm:aff id="aff3"><institution>Commonwealth Scientific and Industrial Research Organization (Australia) Ecosystems Science</institution>, Canberra, ACT 0200,<country>Australia</country></nlm:aff></affiliation></author><author><name sortKey="Meirelles, Tamara" sort="Meirelles, Tamara" uniqKey="Meirelles T" first="Tamara" last="Meirelles">Tamara Meirelles</name><affiliation><nlm:aff id="aff1">Research School of Chemistry,<institution>Australian National University</institution>, Canberra, ACT 0200,<country>Australia</country>;</nlm:aff></affiliation></author><author><name sortKey="Lethier, Mathilde" sort="Lethier, Mathilde" uniqKey="Lethier M" first="Mathilde" last="Lethier">Mathilde Lethier</name><affiliation><nlm:aff wicri:cut="; and" id="aff2"><institution>Institut de Biologie Structurale</institution>, Commissariat a l'Energie Atomique, F-38027 Grenoble,<country>France</country></nlm:aff></affiliation></author><author><name sortKey="Pandey, Gunjan" sort="Pandey, Gunjan" uniqKey="Pandey G" first="Gunjan" last="Pandey">Gunjan Pandey</name><affiliation><nlm:aff id="aff3"><institution>Commonwealth Scientific and Industrial Research Organization (Australia) Ecosystems Science</institution>, Canberra, ACT 0200,<country>Australia</country></nlm:aff></affiliation></author><author><name sortKey="Ollis, David L" sort="Ollis, David L" uniqKey="Ollis D" first="David L." last="Ollis">David L. Ollis</name><affiliation><nlm:aff id="aff1">Research School of Chemistry,<institution>Australian National University</institution>, Canberra, ACT 0200,<country>Australia</country>;</nlm:aff></affiliation></author><author><name sortKey="Russell, Robyn J" sort="Russell, Robyn J" uniqKey="Russell R" first="Robyn J." last="Russell">Robyn J. Russell</name><affiliation><nlm:aff id="aff3"><institution>Commonwealth Scientific and Industrial Research Organization (Australia) Ecosystems Science</institution>, Canberra, ACT 0200,<country>Australia</country></nlm:aff></affiliation></author><author><name sortKey="Weik, Martin" sort="Weik, Martin" uniqKey="Weik M" first="Martin" last="Weik">Martin Weik</name><affiliation><nlm:aff wicri:cut="; and" id="aff2"><institution>Institut de Biologie Structurale</institution>, Commissariat a l'Energie Atomique, F-38027 Grenoble,<country>France</country></nlm:aff></affiliation></author><author><name sortKey="Oakeshott, John G" sort="Oakeshott, John G" uniqKey="Oakeshott J" first="John G." last="Oakeshott">John G. Oakeshott</name><affiliation><nlm:aff id="aff3"><institution>Commonwealth Scientific and Industrial Research Organization (Australia) Ecosystems Science</institution>, Canberra, ACT 0200,<country>Australia</country></nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">23733941</idno><idno type="pmc">3690851</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3690851</idno><idno type="RBID">PMC:3690851</idno><idno type="doi">10.1073/pnas.1304097110</idno><date when="2013">2013</date><idno type="wicri:Area/Pmc/Corpus">001B84</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">001B84</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Structure and function of an insect α-carboxylesterase (α<italic>Esterase</italic>7) associated with insecticide resistance</title><author><name sortKey="Jackson, Colin J" sort="Jackson, Colin J" uniqKey="Jackson C" first="Colin J." last="Jackson">Colin J. Jackson</name><affiliation><nlm:aff id="aff1">Research School of Chemistry,<institution>Australian National University</institution>, Canberra, ACT 0200,<country>Australia</country>;</nlm:aff></affiliation><affiliation><nlm:aff wicri:cut="; and" id="aff2"><institution>Institut de Biologie Structurale</institution>, Commissariat a l'Energie Atomique, F-38027 Grenoble,<country>France</country></nlm:aff></affiliation></author><author><name sortKey="Liu, Jian Wei" sort="Liu, Jian Wei" uniqKey="Liu J" first="Jian-Wei" last="Liu">Jian-Wei Liu</name><affiliation><nlm:aff id="aff3"><institution>Commonwealth Scientific and Industrial Research Organization (Australia) Ecosystems Science</institution>, Canberra, ACT 0200,<country>Australia</country></nlm:aff></affiliation></author><author><name sortKey="Carr, Paul D" sort="Carr, Paul D" uniqKey="Carr P" first="Paul D." last="Carr">Paul D. Carr</name><affiliation><nlm:aff id="aff1">Research School of Chemistry,<institution>Australian National University</institution>, Canberra, ACT 0200,<country>Australia</country>;</nlm:aff></affiliation></author><author><name sortKey="Younus, Faisal" sort="Younus, Faisal" uniqKey="Younus F" first="Faisal" last="Younus">Faisal Younus</name><affiliation><nlm:aff id="aff3"><institution>Commonwealth Scientific and Industrial Research Organization (Australia) Ecosystems Science</institution>, Canberra, ACT 0200,<country>Australia</country></nlm:aff></affiliation></author><author><name sortKey="Coppin, Chris" sort="Coppin, Chris" uniqKey="Coppin C" first="Chris" last="Coppin">Chris Coppin</name><affiliation><nlm:aff id="aff3"><institution>Commonwealth Scientific and Industrial Research Organization (Australia) Ecosystems Science</institution>, Canberra, ACT 0200,<country>Australia</country></nlm:aff></affiliation></author><author><name sortKey="Meirelles, Tamara" sort="Meirelles, Tamara" uniqKey="Meirelles T" first="Tamara" last="Meirelles">Tamara Meirelles</name><affiliation><nlm:aff id="aff1">Research School of Chemistry,<institution>Australian National University</institution>, Canberra, ACT 0200,<country>Australia</country>;</nlm:aff></affiliation></author><author><name sortKey="Lethier, Mathilde" sort="Lethier, Mathilde" uniqKey="Lethier M" first="Mathilde" last="Lethier">Mathilde Lethier</name><affiliation><nlm:aff wicri:cut="; and" id="aff2"><institution>Institut de Biologie Structurale</institution>, Commissariat a l'Energie Atomique, F-38027 Grenoble,<country>France</country></nlm:aff></affiliation></author><author><name sortKey="Pandey, Gunjan" sort="Pandey, Gunjan" uniqKey="Pandey G" first="Gunjan" last="Pandey">Gunjan Pandey</name><affiliation><nlm:aff id="aff3"><institution>Commonwealth Scientific and Industrial Research Organization (Australia) Ecosystems Science</institution>, Canberra, ACT 0200,<country>Australia</country></nlm:aff></affiliation></author><author><name sortKey="Ollis, David L" sort="Ollis, David L" uniqKey="Ollis D" first="David L." last="Ollis">David L. Ollis</name><affiliation><nlm:aff id="aff1">Research School of Chemistry,<institution>Australian National University</institution>, Canberra, ACT 0200,<country>Australia</country>;</nlm:aff></affiliation></author><author><name sortKey="Russell, Robyn J" sort="Russell, Robyn J" uniqKey="Russell R" first="Robyn J." last="Russell">Robyn J. Russell</name><affiliation><nlm:aff id="aff3"><institution>Commonwealth Scientific and Industrial Research Organization (Australia) Ecosystems Science</institution>, Canberra, ACT 0200,<country>Australia</country></nlm:aff></affiliation></author><author><name sortKey="Weik, Martin" sort="Weik, Martin" uniqKey="Weik M" first="Martin" last="Weik">Martin Weik</name><affiliation><nlm:aff wicri:cut="; and" id="aff2"><institution>Institut de Biologie Structurale</institution>, Commissariat a l'Energie Atomique, F-38027 Grenoble,<country>France</country></nlm:aff></affiliation></author><author><name sortKey="Oakeshott, John G" sort="Oakeshott, John G" uniqKey="Oakeshott J" first="John G." last="Oakeshott">John G. Oakeshott</name><affiliation><nlm:aff id="aff3"><institution>Commonwealth Scientific and Industrial Research Organization (Australia) Ecosystems Science</institution>, Canberra, ACT 0200,<country>Australia</country></nlm:aff></affiliation></author></analytic><series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title><idno type="ISSN">0027-8424</idno><idno type="eISSN">1091-6490</idno><imprint><date when="2013">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Insect carboxylesterases from the α<italic>Esterase</italic> gene cluster, such as αE7 (also known as E3) from the Australian sheep blowfly <italic>Lucilia cuprina</italic> (<italic>Lc</italic>αE7), play an important physiological role in lipid metabolism and are implicated in the detoxification of organophosphate (OP) insecticides. Despite the importance of OPs to agriculture and the spread of insect-borne diseases, the molecular basis for the ability of α-carboxylesterases to confer OP resistance to insects is poorly understood. In this work, we used laboratory evolution to increase the thermal stability of <italic>Lc</italic>αE7, allowing its overexpression in <italic>Escherichia coli</italic> and structure determination. The crystal structure reveals a canonical α/β-hydrolase fold that is very similar to the primary target of OPs (acetylcholinesterase) and a unique N-terminal α-helix that serves as a membrane anchor. Soaking of <italic>Lc</italic>αE7 crystals in OPs led to the capture of a crystallographic snapshot of <italic>Lc</italic>αE7 in its phosphorylated state, which allowed comparison with acetylcholinesterase and rationalization of its ability to protect insects against the effects of OPs. Finally, inspection of the active site of <italic>Lc</italic>αE7 reveals an asymmetric and hydrophobic substrate binding cavity that is well-suited to fatty acid methyl esters, which are hydrolyzed by the enzyme with specificity constants (∼10<sup>6</sup> M<sup>−1</sup> s<sup>−1</sup>) indicative of a natural substrate.</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">Proc Natl Acad Sci U S A</journal-id><journal-id journal-id-type="iso-abbrev">Proc. Natl. Acad. Sci. U.S.A</journal-id><journal-id journal-id-type="hwp">pnas</journal-id><journal-id journal-id-type="pmc">pnas</journal-id><journal-id journal-id-type="publisher-id">PNAS</journal-id><journal-title-group><journal-title>Proceedings of the National Academy of Sciences of the United States of America</journal-title></journal-title-group><issn pub-type="ppub">0027-8424</issn><issn pub-type="epub">1091-6490</issn><publisher><publisher-name>National Academy of Sciences</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">23733941</article-id><article-id pub-id-type="pmc">3690851</article-id><article-id pub-id-type="publisher-id">201304097</article-id><article-id pub-id-type="doi">10.1073/pnas.1304097110</article-id><article-categories><subj-group subj-group-type="heading"><subject>Biological Sciences</subject><subj-group><subject>Biochemistry</subject></subj-group></subj-group></article-categories><title-group><article-title>Structure and function of an insect α-carboxylesterase (α<italic>Esterase</italic>7) associated with insecticide resistance</article-title><alt-title alt-title-type="short">Insect α-carboxylesterase structure</alt-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Jackson</surname><given-names>Colin J.</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref><xref ref-type="aff" rid="aff2"><sup>b</sup></xref><xref ref-type="corresp" rid="cor1"><sup>1</sup></xref></contrib><contrib contrib-type="author"><name><surname>Liu</surname><given-names>Jian-Wei</given-names></name><xref ref-type="aff" rid="aff3"><sup>c</sup></xref></contrib><contrib contrib-type="author"><name><surname>Carr</surname><given-names>Paul D.</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref></contrib><contrib contrib-type="author"><name><surname>Younus</surname><given-names>Faisal</given-names></name><xref ref-type="aff" rid="aff3"><sup>c</sup></xref></contrib><contrib contrib-type="author"><name><surname>Coppin</surname><given-names>Chris</given-names></name><xref ref-type="aff" rid="aff3"><sup>c</sup></xref></contrib><contrib contrib-type="author"><name><surname>Meirelles</surname><given-names>Tamara</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref></contrib><contrib contrib-type="author"><name><surname>Lethier</surname><given-names>Mathilde</given-names></name><xref ref-type="aff" rid="aff2"><sup>b</sup></xref></contrib><contrib contrib-type="author"><name><surname>Pandey</surname><given-names>Gunjan</given-names></name><xref ref-type="aff" rid="aff3"><sup>c</sup></xref></contrib><contrib contrib-type="author"><name><surname>Ollis</surname><given-names>David L.</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref></contrib><contrib contrib-type="author"><name><surname>Russell</surname><given-names>Robyn J.</given-names></name><xref ref-type="aff" rid="aff3"><sup>c</sup></xref></contrib><contrib contrib-type="author"><name><surname>Weik</surname><given-names>Martin</given-names></name><xref ref-type="aff" rid="aff2"><sup>b</sup></xref></contrib><contrib contrib-type="author"><name><surname>Oakeshott</surname><given-names>John G.</given-names></name><xref ref-type="aff" rid="aff3"><sup>c</sup></xref></contrib><aff id="aff1"><sup>a</sup>Research School of Chemistry,<institution>Australian National University</institution>, Canberra, ACT 0200,<country>Australia</country>;</aff><aff id="aff2"><sup>b</sup><institution>Institut de Biologie Structurale</institution>, Commissariat a l'Energie Atomique, F-38027 Grenoble,<country>France</country>; and</aff><aff id="aff3"><sup>c</sup><institution>Commonwealth Scientific and Industrial Research Organization (Australia) Ecosystems Science</institution>, Canberra, ACT 0200,<country>Australia</country></aff></contrib-group><author-notes><corresp id="cor1"><sup>1</sup>To whom correspondence should be addressed. E-mail: <email>cjackson@rsc.anu.edu.au</email>.</corresp><fn fn-type="edited-by"><p>Edited by Bruce D. Hammock, University of California, Davis, CA, and approved May 2, 2013 (received for review March 6, 2013)</p></fn><fn fn-type="con"><p>Author contributions: C.J.J., J.-W.L., D.L.O., R.J.R., M.W., and J.G.O. designed research; C.J.J., J.-W.L., P.D.C., F.Y., C.C., T.M., M.L., and G.P. performed research; C.J.J., M.W., and J.G.O. analyzed data; and C.J.J. and J.G.O. wrote the paper.</p></fn></author-notes><pub-date pub-type="ppub"><day>18</day><month>6</month><year>2013</year></pub-date><pub-date pub-type="epub"><day>3</day><month>6</month><year>2013</year></pub-date><pub-date pub-type="pmc-release"><day>3</day><month>6</month><year>2013</year></pub-date><pmc-comment> PMC Release delay is 0 months and 0 days and was based on the
<volume>110</volume><issue>25</issue><fpage>10177</fpage><lpage>10182</lpage><permissions><license license-type="open-access"><license-p>Freely available online through the PNAS open access option.</license-p></license></permissions><self-uri xlink:title="pdf" xlink:type="simple" xlink:href="pnas.201304097.pdf"></self-uri><abstract><p>Insect carboxylesterases from the α<italic>Esterase</italic> gene cluster, such as αE7 (also known as E3) from the Australian sheep blowfly <italic>Lucilia cuprina</italic> (<italic>Lc</italic>αE7), play an important physiological role in lipid metabolism and are implicated in the detoxification of organophosphate (OP) insecticides. Despite the importance of OPs to agriculture and the spread of insect-borne diseases, the molecular basis for the ability of α-carboxylesterases to confer OP resistance to insects is poorly understood. In this work, we used laboratory evolution to increase the thermal stability of <italic>Lc</italic>αE7, allowing its overexpression in <italic>Escherichia coli</italic> and structure determination. The crystal structure reveals a canonical α/β-hydrolase fold that is very similar to the primary target of OPs (acetylcholinesterase) and a unique N-terminal α-helix that serves as a membrane anchor. Soaking of <italic>Lc</italic>αE7 crystals in OPs led to the capture of a crystallographic snapshot of <italic>Lc</italic>αE7 in its phosphorylated state, which allowed comparison with acetylcholinesterase and rationalization of its ability to protect insects against the effects of OPs. Finally, inspection of the active site of <italic>Lc</italic>αE7 reveals an asymmetric and hydrophobic substrate binding cavity that is well-suited to fatty acid methyl esters, which are hydrolyzed by the enzyme with specificity constants (∼10<sup>6</sup> M<sup>−1</sup> s<sup>−1</sup>) indicative of a natural substrate.</p></abstract><kwd-group><kwd>protein engineering</kwd><kwd>directed evolution</kwd><kwd>ali-esterase</kwd></kwd-group><counts><page-count count="6"></page-count></counts></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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