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New page: left|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="450" color="white" frame="true" align="right" spinBox="true"
caption="1txt, resolution 2.501&Aring;" />
'''Staphylococcus aureus 3-hydroxy-3-methylglutaryl-CoA synthase'''<br />


==Overview==
==Staphylococcus aureus 3-hydroxy-3-methylglutaryl-CoA synthase==
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.
<StructureSection load='1txt' size='340' side='right'caption='[[1txt]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1txt]] is a 4 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TXT FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.501&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAA:ACETOACETYL-COENZYME+A'>CAA</scene>, <scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1txt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1txt OCA], [https://pdbe.org/1txt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1txt RCSB], [https://www.ebi.ac.uk/pdbsum/1txt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1txt ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9FD87_STAAU Q9FD87_STAAU]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tx/1txt_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1txt ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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==
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<ref>PMID:15292254</ref>
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TXT OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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]
</div>
[[Category: Hydroxymethylglutaryl-CoA synthase]]
<div class="pdbe-citations 1txt" style="background-color:#fffaf0;"></div>
[[Category: Single protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
[[Category: Campobasso, N.]]
[[Category: Campobasso N]]
[[Category: Gwynn, M.]]
[[Category: Gwynn M]]
[[Category: Kallender, H.]]
[[Category: Kallender H]]
[[Category: Patel, M.]]
[[Category: Patel M]]
[[Category: Rosenberg, M.]]
[[Category: Rosenberg M]]
[[Category: Wilding, I.E.]]
[[Category: Wilding IE]]
[[Category: CAA]]
[[Category: coenzyme a; thiolase fold; condensing enzyme; cholesterol biosynthesis]]
[[Category: hmg-coa synthase; hmgs]]
 
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Latest revision as of 08:51, 6 November 2024

Staphylococcus aureus 3-hydroxy-3-methylglutaryl-CoA synthase

1txt, resolution 2.50Å

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