1txt
From Proteopedia
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|PDB= 1txt |SIZE=350|CAPTION= <scene name='initialview01'>1txt</scene>, resolution 2.501Å | |PDB= 1txt |SIZE=350|CAPTION= <scene name='initialview01'>1txt</scene>, resolution 2.501Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CAA:ACETOACETYL-COENZYME A'>CAA</scene> | + | |LIGAND= <scene name='pdbligand=CAA:ACETOACETYL-COENZYME+A'>CAA</scene>, <scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= mvaS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus]) | |GENE= mvaS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1tvz|1TVZ]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1txt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1txt OCA], [http://www.ebi.ac.uk/pdbsum/1txt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1txt RCSB]</span> | ||
}} | }} | ||
| Line 29: | Line 32: | ||
[[Category: Rosenberg, M.]] | [[Category: Rosenberg, M.]] | ||
[[Category: Wilding, I E.]] | [[Category: Wilding, I E.]] | ||
| - | [[Category: | + | [[Category: cholesterol biosynthesis]] |
| - | [[Category: coenzyme | + | [[Category: coenzyme some]] |
| - | [[Category: hmg-coa synthase | + | [[Category: condensing enzyme]] |
| + | [[Category: hmg-coa synthase]] | ||
| + | [[Category: hmg]] | ||
| + | [[Category: thiolase fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:02:37 2008'' |
Revision as of 21:02, 30 March 2008
| |||||||
| , resolution 2.501Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | mvaS (Staphylococcus aureus) | ||||||
| Activity: | Hydroxymethylglutaryl-CoA synthase, with EC number 2.3.3.10 | ||||||
| Related: | 1TVZ
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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