3kp9

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{{STRUCTURE_3kp9| PDB=3kp9 | SCENE= }}
 
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===Structure of a bacterial homolog of vitamin K epoxide reductase===
 
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{{ABSTRACT_PUBMED_20110994}}
 
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==About this Structure==
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==Structure of a bacterial homolog of vitamin K epoxide reductase==
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[[3kp9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Synechococcus_sp. Synechococcus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KP9 OCA].
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<StructureSection load='3kp9' size='340' side='right'caption='[[3kp9]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3kp9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_sp._JA-2-3B'a(2-13) Synechococcus sp. JA-2-3B'a(2-13)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KP9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KP9 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]] 3.6&#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=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=U10:UBIQUINONE-10'>U10</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=3kp9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kp9 OCA], [https://pdbe.org/3kp9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kp9 RCSB], [https://www.ebi.ac.uk/pdbsum/3kp9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kp9 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/VKOR_SYNJB VKOR_SYNJB] Thiol-disulfide oxidoreductase that catalyzes vitamin K-dependent disulfide bond formation in periplasmic target proteins.<ref>PMID:20110994</ref> <ref>PMID:24477003</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kp/3kp9_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3kp9 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Vitamin K epoxide reductase (VKOR) generates vitamin K hydroquinone to sustain gamma-carboxylation of many blood coagulation factors. Here, we report the 3.6 A crystal structure of a bacterial homologue of VKOR from Synechococcus sp. The structure shows VKOR in complex with its naturally fused redox partner, a thioredoxin-like domain, and corresponds to an arrested state of electron transfer. The catalytic core of VKOR is a four transmembrane helix bundle that surrounds a quinone, connected through an additional transmembrane segment with the periplasmic thioredoxin-like domain. We propose a pathway for how VKOR uses electrons from cysteines of newly synthesized proteins to reduce a quinone, a mechanism confirmed by in vitro reconstitution of vitamin K-dependent disulphide bridge formation. Our results have implications for the mechanism of the mammalian VKOR and explain how mutations can cause resistance to the VKOR inhibitor warfarin, the most commonly used oral anticoagulant.
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==Reference==
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Structure of a bacterial homologue of vitamin K epoxide reductase.,Li W, Schulman S, Dutton RJ, Boyd D, Beckwith J, Rapoport TA Nature. 2010 Jan 28;463(7280):507-12. PMID:20110994<ref>PMID:20110994</ref>
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<ref group="xtra">PMID:020110994</ref><references group="xtra"/><references/>
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[[Category: Synechococcus sp.]]
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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: Beckwith, J.]]
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</div>
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[[Category: Boyd, D.]]
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<div class="pdbe-citations 3kp9" style="background-color:#fffaf0;"></div>
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[[Category: Dutton, R J.]]
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== References ==
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[[Category: Li, W.]]
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<references/>
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[[Category: Rapoport, T A.]]
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__TOC__
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[[Category: Schulman, S.]]
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</StructureSection>
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[[Category: Blood coagulation]]
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[[Category: Large Structures]]
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[[Category: Disulfide formation]]
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[[Category: Beckwith J]]
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[[Category: Oxidoreductase]]
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[[Category: Boyd D]]
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[[Category: Warfarin]]
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[[Category: Dutton RJ]]
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[[Category: Li W]]
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[[Category: Rapoport TA]]
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[[Category: Schulman S]]

Current revision

Structure of a bacterial homolog of vitamin K epoxide reductase

PDB ID 3kp9

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