5hra: Difference between revisions
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==Crystal structure of an aspartate/glutamate racemase in complex with D-aspartate== | |||
<StructureSection load='5hra' size='340' side='right' caption='[[5hra]], [[Resolution|resolution]] 1.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5hra]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HRA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HRA FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DAS:D-ASPARTIC+ACID'>DAS</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5hqt|5hqt]], [[5hrc|5hrc]]</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=5hra FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hra OCA], [http://pdbe.org/5hra PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hra RCSB], [http://www.ebi.ac.uk/pdbsum/5hra PDBsum]</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> | ||
<div class="pdbe-citations 5hra" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Cui, Y]] | |||
[[Category: Gao, F]] | |||
[[Category: Kang, X]] | |||
[[Category: Liu, S]] | |||
[[Category: Liu, X]] | [[Category: Liu, X]] | ||
[[Category: Ma, Y]] | [[Category: Ma, Y]] | ||
[[Category: Yuan, Z]] | [[Category: Yuan, Z]] | ||
[[Category: | [[Category: Aspartate/glutamate racemase]] | ||
[[Category: Isomerase]] | |||
[[Category: Plp-independent racemase]] | |||
[[Category: Racemization mechanism]] | |||
Revision as of 18:48, 12 May 2016
Crystal structure of an aspartate/glutamate racemase in complex with D-aspartate
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