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| '''Staphylococcus aureus 3-hydroxy-3-methylglutaryl-CoA synthase'''
| | ===Staphylococcus aureus 3-hydroxy-3-methylglutaryl-CoA synthase=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15292254}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15292254 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15292254}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Hmg]] | | [[Category: Hmg]] |
| [[Category: Thiolase fold]] | | [[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 Mon Jul 28 09:03:01 2008'' |
