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'''Staphylococcus aureus 3-hydroxy-3-methylglutaryl-CoA synthase''' | {{Structure | ||
|PDB= 1txt |SIZE=350|CAPTION= <scene name='initialview01'>1txt</scene>, resolution 2.501Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CAA:ACETOACETYL-COENZYME A'>CAA</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Hydroxymethylglutaryl-CoA_synthase Hydroxymethylglutaryl-CoA synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.3.10 2.3.3.10] | |||
|GENE= mvaS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus]) | |||
}} | |||
'''Staphylococcus aureus 3-hydroxy-3-methylglutaryl-CoA synthase''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1TXT is a [ | 1TXT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TXT OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15292254 15292254] | ||
[[Category: Hydroxymethylglutaryl-CoA synthase]] | [[Category: Hydroxymethylglutaryl-CoA synthase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: CAA]] | [[Category: CAA]] | ||
[[Category: coenzyme a; thiolase fold; condensing enzyme; cholesterol biosynthesis]] | [[Category: coenzyme a; thiolase fold; condensing enzyme; cholesterol biosynthesis]] | ||
[[Category: hmg-coa synthase; | [[Category: hmg-coa synthase; hmg]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:24:37 2008'' | ||
Revision as of 12:24, 20 March 2008
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| 1txt, resolution 2.501Å | |||||||||||||
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| Ligands: | CAA | ||||||||||||
| Gene: | mvaS (Staphylococcus aureus) | ||||||||||||
| Activity: | Hydroxymethylglutaryl-CoA synthase, with EC number 2.3.3.10 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
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