8zrx: Difference between revisions
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The | ==Structure of human ECHS1 in complex with Acetoacetyl-CoA== | ||
<StructureSection load='8zrx' size='340' side='right'caption='[[8zrx]], [[Resolution|resolution]] 2.27Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8zrx]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8ZRX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ZRX FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.27Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAA:ACETOACETYL-COENZYME+A'>CAA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8zrx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8zrx OCA], [https://pdbe.org/8zrx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8zrx RCSB], [https://www.ebi.ac.uk/pdbsum/8zrx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8zrx ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ECHM_HUMAN ECHM_HUMAN] Straight-chain enoyl-CoA thioesters from C4 up to at least C16 are processed, although with decreasing catalytic rate. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Deficiency of short-chain enoyl-CoA hydratase (ECHS1), a crucial enzyme in fatty acid metabolism through the mitochondrial beta-oxidation pathway, has been strongly linked to various diseases, especially cardiomyopathy. However, the structural and biochemical mechanisms through which ECHS1 recognizes acyl-CoAs remain poorly understood. Herein, cryo-EM analysis reveals the apo structure of ECHS1 and structures of the ECHS1-crotonyl-CoA, ECHS1-acetoacetyl-CoA, ECHS1-hexanoyl-CoA, and ECHS1-octanoyl-CoA complexes at high resolutions. The mechanism through which ECHS1 recognizes its substrates varies with the fatty acid chain lengths of acyl-CoAs. Furthermore, crucial point mutations in ECHS1 have a great impact on substrate recognition, resulting in significant changes in binding affinity and enzyme activity, as do disease-related point mutations in ECHS1. The functional mechanism of ECHS1 is systematically elucidated from structural and biochemical perspectives. These findings provide a theoretical basis for subsequent work focused on determining the role of ECHS1 deficiency (ECHS1D) in the occurrence of diseases such as cardiomyopathy. | |||
Structural and biochemical mechanism of short-chain enoyl-CoA hydratase (ECHS1) substrate recognition.,Su G, Xu Y, Chen B, Ju K, Jin Y, Chen H, Zhang S, Luan X Commun Biol. 2025 Apr 16;8(1):619. doi: 10.1038/s42003-025-07924-0. PMID:40240482<ref>PMID:40240482</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8zrx" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Chen B]] | |||
[[Category: Chen H]] | |||
[[Category: Jin Y]] | |||
[[Category: Ju K]] | |||
[[Category: Liu D]] | |||
[[Category: Luan X]] | |||
[[Category: Su G]] | |||
[[Category: Sun X]] | |||
[[Category: Xu Y]] | |||
[[Category: Zhang S]] | |||
Latest revision as of 10:27, 30 April 2025
Structure of human ECHS1 in complex with Acetoacetyl-CoA
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