5ivi: Difference between revisions
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==The alpha-esterase-7 carboxylesterase, E3, from the blowfly Lucilia cuprina: phosphorylated enzyme qFit multi-conformer model== | ==The alpha-esterase-7 carboxylesterase, E3, from the blowfly Lucilia cuprina: phosphorylated enzyme qFit multi-conformer model== | ||
<StructureSection load='5ivi' size='340' side='right' caption='[[5ivi]], [[Resolution|resolution]] 1.53Å' scene=''> | <StructureSection load='5ivi' size='340' side='right'caption='[[5ivi]], [[Resolution|resolution]] 1.53Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ivi]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IVI OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5ivi]] 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=5IVI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IVI FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.53Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DPF:DIETHYL+HYDROGEN+PHOSPHATE'>DPF</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ivi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ivi OCA], [https://pdbe.org/5ivi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ivi RCSB], [https://www.ebi.ac.uk/pdbsum/5ivi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ivi ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q25252_LUCCU Q25252_LUCCU] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 5ivi" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5ivi" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Carboxylesterase 3D structures|Carboxylesterase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Lucilia cuprina]] | ||
[[Category: | [[Category: Correy GJ]] | ||
[[Category: | [[Category: Jackson CJ]] | ||
Latest revision as of 13:33, 6 September 2023
The alpha-esterase-7 carboxylesterase, E3, from the blowfly Lucilia cuprina: phosphorylated enzyme qFit multi-conformer modelThe alpha-esterase-7 carboxylesterase, E3, from the blowfly Lucilia cuprina: phosphorylated enzyme qFit multi-conformer model
Structural highlights
FunctionPublication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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