5ivh

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'''Unreleased structure'''
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{{Large structure}}
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==The alpha-esterase-7 carboxylesterase, E3, from the blowfly Lucilia cuprina: apo-enzyme ensemble refinement==
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<StructureSection load='5ivh' size='340' side='right' caption='[[5ivh]], [[Resolution|resolution]] 1.71&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5ivh]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IVH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IVH FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ivk|5ivk]], [[5ivd|5ivd]], [[5ivi|5ivi]]</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=5ivh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ivh OCA], [http://pdbe.org/5ivh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ivh RCSB], [http://www.ebi.ac.uk/pdbsum/5ivh PDBsum]</span></td></tr>
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</table>
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{{Large structure}}
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The proper function of enzymes often depends upon their efficient interconversion between particular conformational sub-states on a free-energy landscape. Experimentally characterizing these sub-states is challenging, which has limited our understanding of the role of protein dynamics in many enzymes. Here, we have used a combination of kinetic crystallography and detailed analysis of crystallographic protein ensembles to map the accessible conformational landscape of an insect carboxylesterase (LcalphaE7) as it traverses all steps in its catalytic cycle. LcalphaE7 is of special interest because of its evolving role in organophosphate insecticide resistance. Our results reveal that a dynamically coupled network of residues extends from the substrate-binding site to a surface loop. Interestingly, the coupling of this network that is apparent in the apoenzyme appears to be reduced in the phosphorylated enzyme intermediate. Altogether, the results of this work highlight the importance of protein dynamics to enzyme function and the evolution of new activity.
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The entry 5ivh is ON HOLD
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Mapping the Accessible Conformational Landscape of an Insect Carboxylesterase Using Conformational Ensemble Analysis and Kinetic Crystallography.,Correy GJ, Carr PD, Meirelles T, Mabbitt PD, Fraser NJ, Weik M, Jackson CJ Structure. 2016 Jun 7;24(6):977-87. doi: 10.1016/j.str.2016.04.009. Epub 2016 May, 19. PMID:27210287<ref>PMID:27210287</ref>
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Authors: Correy, G.J., Jackson, C.J.
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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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Description: The alpha-esterase-7 carboxylesterase, E3, from the blowfly Lucilia cuprina: apo-enzyme ensemble refinement
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<div class="pdbe-citations 5ivh" style="background-color:#fffaf0;"></div>
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[[Category: Unreleased Structures]]
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== References ==
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[[Category: Jackson, C.J]]
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<references/>
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[[Category: Correy, G.J]]
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__TOC__
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</StructureSection>
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[[Category: Correy, G J]]
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[[Category: Jackson, C J]]
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[[Category: Acetylcholinesterase]]
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[[Category: Carboxylesterase]]
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[[Category: Hydrolase]]
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[[Category: Organophosphate]]
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[[Category: Protein dynamic]]

Revision as of 23:08, 23 June 2016

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The alpha-esterase-7 carboxylesterase, E3, from the blowfly Lucilia cuprina: apo-enzyme ensemble refinement

5ivh, resolution 1.71Å

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