4mh1: Difference between revisions
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The | ==Crystal structure and functional studies of quinoprotein L-sorbose dehydrogenase from Ketogulonicigenium vulgare Y25== | ||
<StructureSection load='4mh1' size='340' side='right'caption='[[4mh1]], [[Resolution|resolution]] 2.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4mh1]] is a 2 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=4MH1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MH1 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]] 2.7Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PQQ:PYRROLOQUINOLINE+QUINONE'>PQQ</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=4mh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mh1 OCA], [https://pdbe.org/4mh1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mh1 RCSB], [https://www.ebi.ac.uk/pdbsum/4mh1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mh1 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The crystal structure of the L-sorbose dehydrogenase (SDH) from Ketogulonicigenium vulgare Y25 has been determined at 2.7 A resolution using the molecular replacement method. The overall structure of SDH is similar to that of other quinoprotein dehydrogenases; consisting of an eight bladed beta-propeller PQQ domain and protrusion loops. We identified a stable homodimer in crystal and demonstrated its existence in solution by sedimentation velocity measurement. By biochemical characterization of the SDH in vitro, using L-sorbose as substrate and cytochrome c551 as electron acceptor, we revealed cytochrome c551 acting as physiological primary electron acceptor for SDH. | |||
Crystal structure of L-sorbose dehydrogenase, a pyrroloquinoline quinone-dependent enzyme with homodimeric assembly, from Ketogulonicigenium vulgare.,Han X, Xiong X, Jiang D, Chen S, Huang E, Zhang W, Liu X Biotechnol Lett. 2014 May;36(5):1001-8. doi: 10.1007/s10529-013-1446-5. Epub 2014, Feb 21. PMID:24557074<ref>PMID:24557074</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4mh1" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Ketogulonicigenium vulgare Y25]] | |||
[[Category: Large Structures]] | |||
[[Category: Han X]] | |||
[[Category: Liu X]] | |||
Latest revision as of 14:43, 8 November 2023
Crystal structure and functional studies of quinoprotein L-sorbose dehydrogenase from Ketogulonicigenium vulgare Y25
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