1txt
From Proteopedia
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Staphylococcus aureus 3-hydroxy-3-methylglutaryl-CoA synthase
Overview
3-Hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) synthase, a member of the, family of acyl-condensing enzymes, catalyzes the first committed step in, the mevalonate pathway and is a potential target for novel antibiotics and, cholesterol-lowering agents. The Staphylococcus aureus mvaS gene product, (43.2 kDa) was overexpressed in Escherichia coli, purified to homogeneity, and shown biochemically to be an HMG-CoA synthase. The crystal structure, of the full-length enzyme was determined at 2.0-A resolution, representing, the first structure of an HMG-CoA synthase from any organism. HMG-CoA, synthase forms a homodimer. The monomer, however, contains an important, core structure of two similar alpha/beta motifs, a fold that is completely, conserved among acyl-condensing enzymes. This common fold provides a, scaffold for a catalytic triad made up of Cys, His, and Asn required by, these enzymes. In addition, a crystal structure of HMG-CoA synthase with, acetoacetyl-CoA was determined at 2.5-A resolution. Together, these, structures provide the structural basis for an understanding of the, mechanism of HMG-CoA synthase.
About this Structure
1TXT is a Single protein structure of sequence from Staphylococcus aureus with CAA as ligand. Active as Hydroxymethylglutaryl-CoA synthase, with EC number 2.3.3.10 Full crystallographic information is available from OCA.
Reference
Staphylococcus aureus 3-hydroxy-3-methylglutaryl-CoA synthase: crystal structure and mechanism., Campobasso N, Patel M, Wilding IE, Kallender H, Rosenberg M, Gwynn MN, J Biol Chem. 2004 Oct 22;279(43):44883-8. Epub 2004 Aug 2. PMID:15292254
Page seeded by OCA on Sun Nov 25 02:56:44 2007
