View source for 5hrc


==Crystal structure of an aspartate/glutamate racemase in complex with L-aspartate==
<StructureSection load='5hrc' size='340' side='right'caption='[[5hrc]], [[Resolution|resolution]] 1.77&Aring;' 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]] 1.765&#8491;</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>
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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5hrc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Escherichia coli O157:H7 str. SS52]]
[[Category: Large Structures]]
[[Category: Cui Y]]
[[Category: Gao F]]
[[Category: Kang X]]
[[Category: Liu S]]
[[Category: Liu X]]
[[Category: Ma Y]]
[[Category: Yuan Z]]