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5hqt
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of an aspartate/glutamate racemase from Escherichia coli O157== | |
| + | <StructureSection load='5hqt' size='340' side='right' caption='[[5hqt]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5hqt]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HQT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HQT FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5hra|5hra]], [[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=5hqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hqt OCA], [http://pdbe.org/5hqt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hqt RCSB], [http://www.ebi.ac.uk/pdbsum/5hqt 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> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5hqt" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Cui, Y]] | [[Category: Cui, Y]] | ||
| - | [[Category: Liu, S]] | ||
[[Category: Gao, F]] | [[Category: Gao, F]] | ||
| - | [[Category: Yuan, Z]] | ||
[[Category: Kang, X]] | [[Category: Kang, X]] | ||
| + | [[Category: Liu, S]] | ||
| + | [[Category: Liu, X]] | ||
| + | [[Category: Ma, Y]] | ||
| + | [[Category: Yuan, Z]] | ||
| + | [[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 from Escherichia coli O157
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