5hrc: Difference between revisions
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New page: '''Unreleased structure''' The entry 5hrc is ON HOLD Authors: Liu, X., Gao, F., Ma, Y., Liu, S., Cui, Y., Yuan, Z., Kang, X. Description: Crystal structure of an aspartate/glutamate ra... |
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==Crystal structure of an aspartate/glutamate racemase in complex with L-aspartate== | |||
<StructureSection load='5hrc' size='340' side='right'caption='[[5hrc]], [[Resolution|resolution]] 1.77Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5hrc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7_str._SS52 Escherichia coli O157:H7 str. SS52]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HRC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HRC FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.765Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene>, <scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</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=5hrc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hrc OCA], [https://pdbe.org/5hrc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hrc RCSB], [https://www.ebi.ac.uk/pdbsum/5hrc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hrc ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
EcL-DER, the aspartate/glutamate racemase from the pathogen Escherichia coli O157, exhibits racemase activity for l-aspartate and l-glutamate. This study reports the crystal structures of apo-EcL-DER, the EcL-DER-l-aspartate and the EcL-DER-d-aspartate complexes. The EcL-DER structure contains two domains, forming pseudo-mirror symmetry in the active site. A unique catalytic pair consisting of Thr(83) and Cys(197) exists in the active site. The characteristic conformations of l-Asp and d-Asp in the active site provide a straight structural evidence for the racemization mechanism of EcL-DER. In addition, the diversity of catalytic pairs implies that PLP-independent amino acid racemases adopt various catalytic mechanisms and are classified into different subgroups. | |||
Crystal structure and molecular mechanism of an aspartate/glutamate racemase from Escherichia coli O157.,Liu X, Gao F, Ma Y, Liu S, Cui Y, Yuan Z, Kang X FEBS Lett. 2016 Apr;590(8):1262-9. doi: 10.1002/1873-3468.12148. Epub 2016 Apr 5. PMID:27001440<ref>PMID:27001440</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5hrc" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: Liu | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli O157:H7 str. SS52]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Cui Y]] | |||
[[Category: Gao F]] | |||
[[Category: Kang X]] | |||
[[Category: Liu S]] | |||
[[Category: Liu X]] | |||
[[Category: Ma Y]] | |||
[[Category: Yuan Z]] | |||
Latest revision as of 10:51, 16 August 2023
Crystal structure of an aspartate/glutamate racemase in complex with L-aspartate
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