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5hqt

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'''Unreleased structure'''
 
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The entry 5hqt is ON HOLD
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==Crystal structure of an aspartate/glutamate racemase from Escherichia coli O157==
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<StructureSection load='5hqt' size='340' side='right'caption='[[5hqt]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5hqt]] is a 1 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=5HQT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HQT FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.598&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5hqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hqt OCA], [https://pdbe.org/5hqt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hqt RCSB], [https://www.ebi.ac.uk/pdbsum/5hqt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hqt ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Liu, X., Gao, F., Ma, Y., Liu, S., Cui, Y., Yuan, Z., Kang, X.
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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>
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Description: Crystal structure of an aspartate/glutamate racemase from Escherichia coli O157
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Liu, X]]
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<div class="pdbe-citations 5hqt" style="background-color:#fffaf0;"></div>
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[[Category: Ma, Y]]
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== References ==
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[[Category: Cui, Y]]
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<references/>
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[[Category: Liu, S]]
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__TOC__
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[[Category: Gao, F]]
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</StructureSection>
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[[Category: Yuan, Z]]
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[[Category: Escherichia coli O157:H7 str. SS52]]
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[[Category: Kang, X]]
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[[Category: Large Structures]]
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[[Category: Cui Y]]
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[[Category: Gao F]]
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[[Category: Kang X]]
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[[Category: Liu S]]
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[[Category: Liu X]]
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[[Category: Ma Y]]
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[[Category: Yuan Z]]

Current revision

Crystal structure of an aspartate/glutamate racemase from Escherichia coli O157

PDB ID 5hqt

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