1txt
From Proteopedia
Line 1: | Line 1: | ||
[[Image:1txt.jpg|left|200px]] | [[Image:1txt.jpg|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_1txt", creates the "Structure Box" on the page. | |
- | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
- | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
- | + | or leave the SCENE parameter empty for the default display. | |
- | | | + | --> |
- | | | + | {{STRUCTURE_1txt| PDB=1txt | SCENE= }} |
- | + | ||
- | + | ||
- | }} | + | |
'''Staphylococcus aureus 3-hydroxy-3-methylglutaryl-CoA synthase''' | '''Staphylococcus aureus 3-hydroxy-3-methylglutaryl-CoA synthase''' | ||
Line 32: | Line 29: | ||
[[Category: Rosenberg, M.]] | [[Category: Rosenberg, M.]] | ||
[[Category: Wilding, I E.]] | [[Category: Wilding, I E.]] | ||
- | [[Category: | + | [[Category: Cholesterol biosynthesis]] |
- | [[Category: | + | [[Category: Coenzyme some]] |
- | [[Category: | + | [[Category: Condensing enzyme]] |
- | [[Category: | + | [[Category: Hmg-coa synthase]] |
- | [[Category: | + | [[Category: Hmg]] |
- | [[Category: | + | [[Category: Thiolase fold]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:30:02 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 07:30, 3 May 2008
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. 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 Sat May 3 10:30:02 2008