4lsw
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystallization and Structural Analysis of 2-Hydroxyacid Dehydrogenase from Ketogulonicigenium vulgare Y25== | |
| + | <StructureSection load='4lsw' size='340' side='right'caption='[[4lsw]], [[Resolution|resolution]] 1.64Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4lsw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ketogulonicigenium_vulgare_Y25 Ketogulonicigenium vulgare Y25]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LSW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LSW 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]] 1.64Å</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=4lsw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lsw OCA], [https://pdbe.org/4lsw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lsw RCSB], [https://www.ebi.ac.uk/pdbsum/4lsw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lsw ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | L-2-Hydroxyacid dehydrogenase (HDH) from Ketogulonicigenium vulgare Y25 was cloned and overexpressed in Escherichia coli. The protein was purified and crystallized by the sitting-drop vapour-diffusion method with polyethylene glycol 3350 as precipitant. The crystal structure of HDH was determined at 1.64 A resolution using the molecular replacement method with the crystal structure of hydroxyl (phenyl) pyruvate reductase from Coleus blumei Benth as the search model. The overall structure of HDH was similar to that of hydroxyl(phenyl)pyruvate reductase, consisting of two compact domains separated by a deep active cleft. The most significant structural divergence is located around the pocket gate comprising residues A210, T211 and R212, which is located on top of the catalytic triad. | ||
| - | + | Crystallization and structural analysis of 2-hydroxyacid dehydrogenase from Ketogulonicigenium vulgare.,Han X, Xiong X, Hu X, Li M, Zhang W, Liu X Biotechnol Lett. 2014 Feb;36(2):295-300. doi: 10.1007/s10529-013-1354-8. Epub, 2013 Sep 26. PMID:24068509<ref>PMID:24068509</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4lsw" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Ketogulonicigenium vulgare Y25]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Han X]] | ||
| + | [[Category: Liu X]] | ||
Current revision
Crystallization and Structural Analysis of 2-Hydroxyacid Dehydrogenase from Ketogulonicigenium vulgare Y25
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