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2f82
From Proteopedia
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| - | [[Image:2f82.gif|left|200px]]<br /><applet load="2f82" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2f82, resolution 2.10Å" /> | ||
| - | '''HMG-CoA synthase from Brassica juncea in the apo-form'''<br /> | ||
| - | == | + | ==HMG-CoA synthase from Brassica juncea in the apo-form== |
| + | <StructureSection load='2f82' size='340' side='right'caption='[[2f82]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2f82]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Brassica_juncea Brassica juncea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F82 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F82 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]] 2.1Å</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=2f82 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f82 OCA], [https://pdbe.org/2f82 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f82 RCSB], [https://www.ebi.ac.uk/pdbsum/2f82 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f82 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q9M6U3_BRAJU Q9M6U3_BRAJU] | ||
| + | == 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/f8/2f82_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2f82 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
3-Hydroxy-3-methylglutaryl CoA synthase (HMGS) catalyzes the first committed step in the mevalonate metabolic pathway for isoprenoid biosynthesis and serves as an alternative target for cholesterol-lowering and antibiotic drugs. We have determined a previously undescribed crystal structure of a eukaryotic HMGS bound covalently to a potent and specific inhibitor F-244 [(E,E)-11-[3-(hydroxymethyl)-4-oxo-2-oxytanyl]-3,5,7-trimethyl-2,4-undecad ienenoic acid]. Given the accessibility of synthetic analogs of the F-244 natural product, this inhibited eukaryotic HMGS structure serves as a necessary starting point for structure-based methods that may improve the potency and species-specific selectivity of the next generation of F-244 analogs designed to target particular eukaryotic and prokaryotic HMGS. | 3-Hydroxy-3-methylglutaryl CoA synthase (HMGS) catalyzes the first committed step in the mevalonate metabolic pathway for isoprenoid biosynthesis and serves as an alternative target for cholesterol-lowering and antibiotic drugs. We have determined a previously undescribed crystal structure of a eukaryotic HMGS bound covalently to a potent and specific inhibitor F-244 [(E,E)-11-[3-(hydroxymethyl)-4-oxo-2-oxytanyl]-3,5,7-trimethyl-2,4-undecad ienenoic acid]. Given the accessibility of synthetic analogs of the F-244 natural product, this inhibited eukaryotic HMGS structure serves as a necessary starting point for structure-based methods that may improve the potency and species-specific selectivity of the next generation of F-244 analogs designed to target particular eukaryotic and prokaryotic HMGS. | ||
| - | + | Structural basis for the design of potent and species-specific inhibitors of 3-hydroxy-3-methylglutaryl CoA synthases.,Pojer F, Ferrer JL, Richard SB, Nagegowda DA, Chye ML, Bach TJ, Noel JP Proc Natl Acad Sci U S A. 2006 Aug 1;103(31):11491-6. Epub 2006 Jul 24. PMID:16864776<ref>PMID:16864776</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 2f82" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Brassica juncea]] | [[Category: Brassica juncea]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Ferrer | + | [[Category: Ferrer JL]] |
| - | [[Category: Noel | + | [[Category: Noel JP]] |
| - | [[Category: Pojer | + | [[Category: Pojer F]] |
| - | [[Category: Richard | + | [[Category: Richard SB]] |
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
HMG-CoA synthase from Brassica juncea in the apo-form
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