5hra
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==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 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=5HRA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HRA 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]] 1.597Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DAS:D-ASPARTIC+ACID'>DAS</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=5hra FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hra OCA], [https://pdbe.org/5hra PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hra RCSB], [https://www.ebi.ac.uk/pdbsum/5hra PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hra 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 5hra" 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]] | ||
Current revision
Crystal structure of an aspartate/glutamate racemase in complex with D-aspartate
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Categories: Escherichia coli O157:H7 str. SS52 | Large Structures | Cui Y | Gao F | Kang X | Liu S | Liu X | Ma Y | Yuan Z
