1txt
From Proteopedia
(New page: 200px<br /><applet load="1txt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1txt, resolution 2.501Å" /> '''Staphylococcus aure...) |
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| - | [[Image:1txt.jpg|left|200px]]<br /><applet load="1txt" size=" | + | [[Image:1txt.jpg|left|200px]]<br /><applet load="1txt" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1txt, resolution 2.501Å" /> | caption="1txt, resolution 2.501Å" /> | ||
'''Staphylococcus aureus 3-hydroxy-3-methylglutaryl-CoA synthase'''<br /> | '''Staphylococcus aureus 3-hydroxy-3-methylglutaryl-CoA synthase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | 3-Hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) synthase, a member of the | + | 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== | ==About this Structure== | ||
| - | 1TXT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with CAA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | + | 1TXT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with <scene name='pdbligand=CAA:'>CAA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TXT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Patel, M.]] | [[Category: Patel, M.]] | ||
[[Category: Rosenberg, M.]] | [[Category: Rosenberg, M.]] | ||
| - | [[Category: Wilding, I | + | [[Category: Wilding, I E.]] |
[[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; hmgs]] | [[Category: hmg-coa synthase; hmgs]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:18:36 2008'' |
Revision as of 13:18, 21 February 2008
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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 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
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