1txt

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[[Image:1txt.jpg|left|200px]]<br /><applet load="1txt" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1txt.jpg|left|200px]]
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caption="1txt, resolution 2.501&Aring;" />
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'''Staphylococcus aureus 3-hydroxy-3-methylglutaryl-CoA synthase'''<br />
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{{Structure
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|PDB= 1txt |SIZE=350|CAPTION= <scene name='initialview01'>1txt</scene>, resolution 2.501&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CAA:ACETOACETYL-COENZYME A'>CAA</scene>
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|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]
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|GENE= mvaS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus])
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}}
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'''Staphylococcus aureus 3-hydroxy-3-methylglutaryl-CoA synthase'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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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==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15292254 15292254]
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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]]
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[[Category: hmg-coa synthase; hmgs]]
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[[Category: hmg-coa synthase; hmg]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:18:36 2008''
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''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


PDB ID 1txt

Drag the structure with the mouse to rotate
, resolution 2.501Å
Ligands:
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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