1qax

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[[Image:1qax.png|left|200px]]
 
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==TERNARY COMPLEX OF PSEUDOMONAS MEVALONII HMG-COA REDUCTASE WITH HMG-COA AND NAD+==
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The line below this paragraph, containing "STRUCTURE_1qax", creates the "Structure Box" on the page.
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<StructureSection load='1qax' size='340' side='right'caption='[[1qax]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1qax]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_mevalonii Pseudomonas mevalonii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QAX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QAX 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]] 2.8&#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=HMG:3-HYDROXY-3-METHYLGLUTARYL-COENZYME+A'>HMG</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
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{{STRUCTURE_1qax| PDB=1qax | SCENE= }}
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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=1qax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qax OCA], [https://pdbe.org/1qax PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qax RCSB], [https://www.ebi.ac.uk/pdbsum/1qax PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qax ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MVAA_PSEMV MVAA_PSEMV] P.mevalonii can use mevalonate as sole carbon source. With this enzyme mevalonate is deacetylated to HMG-CoA.
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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/qa/1qax_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=1qax 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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3-hydroxy-3-methylglutaryl-CoA (HMG-CoA) reductase is the rate-limiting enzyme and the first committed step in the biosynthesis of cholesterol in mammals. We have determined the crystal structures of two nonproductive ternary complexes of HMG-CoA reductase, HMG-CoA/NAD+ and mevalonate/NADH, at 2.8 A resolution. In the structure of the Pseudomonas mevalonii apoenzyme, the last 50 residues of the C terminus (the flap domain), including the catalytic residue His381, were not visible. The structures of the ternary complexes reported here reveal a substrate-induced closing of the flap domain that completes the active site and aligns the catalytic histidine proximal to the thioester of HMG-CoA. The structures also present evidence that Lys267 is critically involved in catalysis and provide insights into the catalytic mechanism.
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===TERNARY COMPLEX OF PSEUDOMONAS MEVALONII HMG-COA REDUCTASE WITH HMG-COA AND NAD+===
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Substrate-induced closure of the flap domain in the ternary complex structures provides insights into the mechanism of catalysis by 3-hydroxy-3-methylglutaryl-CoA reductase.,Tabernero L, Bochar DA, Rodwell VW, Stauffacher CV Proc Natl Acad Sci U S A. 1999 Jun 22;96(13):7167-71. PMID:10377386<ref>PMID:10377386</ref>
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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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The line below this paragraph, {{ABSTRACT_PUBMED_10377386}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1qax" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 10377386 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10377386}}
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==About this Structure==
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[[1qax]] is a 2 chain structure of [[HMG-CoA Reductase]] with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_mevalonii Pseudomonas mevalonii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QAX OCA].
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==See Also==
==See Also==
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*[[HMG-CoA Reductase|HMG-CoA Reductase]]
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*[[HMG-CoA Reductase 3D structures|HMG-CoA Reductase 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:010377386</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Pseudomonas mevalonii]]
[[Category: Pseudomonas mevalonii]]
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[[Category: Bochar, D A.]]
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[[Category: Bochar DA]]
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[[Category: Rodwell, V W.]]
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[[Category: Rodwell VW]]
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[[Category: Stauffacher, C V.]]
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[[Category: Stauffacher CV]]
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[[Category: Tabernero, L.]]
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[[Category: Tabernero L]]
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[[Category: 4-electron oxido-reductase]]
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[[Category: Oxidoreductase]]
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Current revision

TERNARY COMPLEX OF PSEUDOMONAS MEVALONII HMG-COA REDUCTASE WITH HMG-COA AND NAD+

PDB ID 1qax

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