1qay

<table><tr><td colspan='2'>[[1qay]] is a 2 chain structure 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=1QAY OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1QAY FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MEV:(R)-MEVALONATE'>MEV</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MVAA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=32044 'Pseudomonas mevalonii'])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1qay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qay OCA], [http://pdbe.org/1qay PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qay RCSB], [http://www.ebi.ac.uk/pdbsum/1qay PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qay ProSAT]</span></td></tr>

[[http://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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== Publication Abstract from PubMed ==

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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1qay" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Bochar, D A]]

[[Category: Rodwell, V W]]

[[Category: Stauffacher, C V]]

[[Category: Tabernero, L]]

[[Category: Oxidoreductase]]