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4fng

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==The alpha-esterase-7 carboxylesterase, E3, from the blowfly Lucilia cuprina==
==The alpha-esterase-7 carboxylesterase, E3, from the blowfly Lucilia cuprina==
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<StructureSection load='4fng' size='340' side='right' caption='[[4fng]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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<StructureSection load='4fng' size='340' side='right'caption='[[4fng]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4fng]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Australian_sheep_blowfly Australian sheep blowfly]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FNG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FNG FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4fng]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lucilia_cuprina Lucilia cuprina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FNG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FNG FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4fg5|4fg5]], [[4fnm|4fnm]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LcaE7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7375 Australian sheep blowfly])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4fng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fng OCA], [https://pdbe.org/4fng PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fng RCSB], [https://www.ebi.ac.uk/pdbsum/4fng PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fng ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fng OCA], [http://pdbe.org/4fng PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fng RCSB], [http://www.ebi.ac.uk/pdbsum/4fng PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fng ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q25252_LUCCU Q25252_LUCCU]
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Insect carboxylesterases from the alphaEsterase gene cluster, such as alphaE7 (also known as E3) from the Australian sheep blowfly Lucilia cuprina (LcalphaE7), 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 alpha-carboxylesterases to confer OP resistance to insects is poorly understood. In this work, we used laboratory evolution to increase the thermal stability of LcalphaE7, allowing its overexpression in Escherichia coli and structure determination. The crystal structure reveals a canonical alpha/beta-hydrolase fold that is very similar to the primary target of OPs (acetylcholinesterase) and a unique N-terminal alpha-helix that serves as a membrane anchor. Soaking of LcalphaE7 crystals in OPs led to the capture of a crystallographic snapshot of LcalphaE7 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 LcalphaE7 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 ( approximately 10(6) M(-1) s(-1)) indicative of a natural substrate.
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Structure and function of an insect alpha-carboxylesterase (alphaEsterase7) associated with insecticide resistance.,Jackson CJ, Liu JW, Carr PD, Younus F, Coppin C, Meirelles T, Lethier M, Pandey G, Ollis DL, Russell RJ, Weik M, Oakeshott JG Proc Natl Acad Sci U S A. 2013 Jun 18;110(25):10177-82. doi:, 10.1073/pnas.1304097110. Epub 2013 Jun 3. PMID:23733941<ref>PMID:23733941</ref>
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==See Also==
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*[[Carboxylesterase 3D structures|Carboxylesterase 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4fng" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Australian sheep blowfly]]
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[[Category: Large Structures]]
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[[Category: Carr, P D]]
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[[Category: Lucilia cuprina]]
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[[Category: Coppin, C]]
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[[Category: Carr PD]]
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[[Category: Jackson, C J]]
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[[Category: Coppin C]]
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[[Category: Liu, J W]]
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[[Category: Jackson CJ]]
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[[Category: Meirelles, T]]
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[[Category: Liu J-W]]
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[[Category: Oakeshott, J G]]
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[[Category: Meirelles T]]
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[[Category: Ollis, D L]]
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[[Category: Oakeshott JG]]
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[[Category: Pandey, G]]
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[[Category: Ollis DL]]
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[[Category: Tawfik, D S]]
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[[Category: Pandey G]]
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[[Category: Weik, M]]
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[[Category: Tawfik DS]]
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[[Category: Younis, F]]
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[[Category: Weik M]]
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[[Category: Alpha/beta hydrolase fold]]
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[[Category: Younis F]]
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[[Category: Carboxylesterase]]
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[[Category: Hydrolase]]
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Current revision

The alpha-esterase-7 carboxylesterase, E3, from the blowfly Lucilia cuprina

PDB ID 4fng

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