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4mh1

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'''Unreleased structure'''
 
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The entry 4mh1 is ON HOLD until Paper Publication
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==Crystal structure and functional studies of quinoprotein L-sorbose dehydrogenase from Ketogulonicigenium vulgare Y25==
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<StructureSection load='4mh1' size='340' side='right'caption='[[4mh1]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<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>
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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]] 2.7&#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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PQQ:PYRROLOQUINOLINE+QUINONE'>PQQ</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=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>
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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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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.
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Authors: Han, X., Liu, X.
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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>
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Description: Crystal structure and functional studies of quinoprotein L-sorbose dehydrogenase from Ketogulonicigenium vulgare Y25
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4mh1" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Ketogulonicigenium vulgare Y25]]
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[[Category: Large Structures]]
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[[Category: Han X]]
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[[Category: Liu X]]

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Crystal structure and functional studies of quinoprotein L-sorbose dehydrogenase from Ketogulonicigenium vulgare Y25

PDB ID 4mh1

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