3kp8: Difference between revisions
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< | ==The thioredoxin-like domain of a VKOR homolog from Synechococcus sp.== | ||
<StructureSection load='3kp8' size='340' side='right'caption='[[3kp8]], [[Resolution|resolution]] 1.66Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3kp8]] 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=3KP8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KP8 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]] 1.66Å</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=3kp8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kp8 OCA], [https://pdbe.org/3kp8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kp8 RCSB], [https://www.ebi.ac.uk/pdbsum/3kp8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kp8 ProSAT]</span></td></tr> | |||
</table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kp/3kp8_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=3kp8 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3kp8" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
[[Category: Beckwith J]] | |||
[[Category: Boyd D]] | |||
== | [[Category: Dutton RJ]] | ||
< | [[Category: Li W]] | ||
[[Category: | [[Category: Rapoport TA]] | ||
[[Category: Beckwith | [[Category: Schulman S]] | ||
[[Category: Boyd | |||
[[Category: Dutton | |||
[[Category: Li | |||
[[Category: Rapoport | |||
[[Category: Schulman | |||
Latest revision as of 05:01, 21 November 2024
The thioredoxin-like domain of a VKOR homolog from Synechococcus sp.The thioredoxin-like domain of a VKOR homolog from Synechococcus sp.
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedVitamin 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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