5ivd: Difference between revisions
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The | ==The alpha-esterase-7 carboxylesterase, E3, from the blowfly Lucilia cuprina: apo-enzyme qFit multi-conformer model== | ||
<StructureSection load='5ivd' size='340' side='right' caption='[[5ivd]], [[Resolution|resolution]] 1.71Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5ivd]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IVD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IVD FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ivh|5ivh]], [[5ivi|5ivi]], [[5ivk|5ivk]]</td></tr> | |||
<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=5ivd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ivd OCA], [http://pdbe.org/5ivd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ivd RCSB], [http://www.ebi.ac.uk/pdbsum/5ivd PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Jackson, C | <div class="pdbe-citations 5ivd" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Correy, G J]] | |||
[[Category: Jackson, C J]] | |||
[[Category: Acetylcholinesterase]] | |||
[[Category: Carboxylesterase]] | |||
[[Category: Hydrolase]] | |||
[[Category: Organophosphate]] | |||
[[Category: Protein dynamic]] | |||
Revision as of 18:12, 20 June 2016
The alpha-esterase-7 carboxylesterase, E3, from the blowfly Lucilia cuprina: apo-enzyme qFit multi-conformer modelThe alpha-esterase-7 carboxylesterase, E3, from the blowfly Lucilia cuprina: apo-enzyme qFit multi-conformer model
Structural highlights
Publication 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. References
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