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Structure and function of an insect α-carboxylesterase (αEsterase7) associated with insecticide resistance

Identifieur interne : 001B84 ( Pmc/Corpus ); précédent : 001B83; suivant : 001B85

Structure and function of an insect α-carboxylesterase (αEsterase7) associated with insecticide resistance

Auteurs : Colin J. Jackson ; Jian-Wei Liu ; Paul D. Carr ; Faisal Younus ; Chris Coppin ; Tamara Meirelles ; Mathilde Lethier ; Gunjan Pandey ; David L. Ollis ; Robyn J. Russell ; Martin Weik ; John G. Oakeshott

Source :

RBID : PMC:3690851

Abstract

Insect carboxylesterases from the αEsterase gene cluster, such as αE7 (also known as E3) from the Australian sheep blowfly Lucilia cuprina (LcαE7), 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 LcαE7, allowing its overexpression in Escherichia coli 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 LcαE7 crystals in OPs led to the capture of a crystallographic snapshot of LcαE7 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 LcαE7 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 (∼106 M−1 s−1) indicative of a natural substrate.


Url:
DOI: 10.1073/pnas.1304097110
PubMed: 23733941
PubMed Central: 3690851

Links to Exploration step

PMC:3690851

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<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>
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<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>
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<subject>Biochemistry</subject>
</subj-group>
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</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 . </pmc-comment>
<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>

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Ou

HfdSelect -h $EXPLOR_AREA/Data/Pmc/Corpus/biblio.hfd -nk 001B84 | SxmlIndent | more

Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Wicri/Asie
   |area=    AustralieFrV1
   |flux=    Pmc
   |étape=   Corpus
   |type=    RBID
   |clé=     PMC:3690851
   |texte=   Structure and function of an insect α-carboxylesterase (αEsterase7) associated with insecticide resistance
}}

Pour générer des pages wiki

HfdIndexSelect -h $EXPLOR_AREA/Data/Pmc/Corpus/RBID.i   -Sk "pubmed:23733941" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/Pmc/Corpus/biblio.hfd   \
       | NlmPubMed2Wicri -a AustralieFrV1
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This area was generated with Dilib version V0.6.33.
Data generation: Tue Dec 5 10:43:12 2017. Site generation: Tue Mar 5 14:07:20 2024