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| - | [[Image:1x9e.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1x9e| PDB=1x9e | SCENE= }} | | {{STRUCTURE_1x9e| PDB=1x9e | SCENE= }} |
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| - | '''Crystal structure of HMG-CoA synthase from Enterococcus faecalis'''
| + | ===Crystal structure of HMG-CoA synthase from Enterococcus faecalis=== |
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| - | ==Overview==
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| - | Biosynthesis of the isoprenoid precursor, isopentenyl diphosphate, is a critical function in all independently living organisms. There are two major pathways for this synthesis, the non-mevalonate pathway found in most eubacteria and the mevalonate pathway found in animal cells and a number of pathogenic bacteria. An early step in this pathway is the condensation of acetyl-CoA and acetoacetyl-CoA into HMG-CoA, catalyzed by the enzyme HMG-CoA synthase. To explore the possibility of a small molecule inhibitor of the enzyme functioning as a non-cell wall antibiotic, the structure of HMG-CoA synthase from Enterococcus faecalis (MVAS) was determined by selenomethionine MAD phasing to 2.4 A and the enzyme complexed with its second substrate, acetoacetyl-CoA, to 1.9 A. These structures show that HMG-CoA synthase from Enterococcus is a member of the family of thiolase fold enzymes and, while similar to the recently published HMG-CoA synthase structures from Staphylococcus aureus, exhibit significant differences in the structure of the C-terminal domain. The acetoacetyl-CoA binary structure demonstrates reduced coenzyme A and acetoacetate covalently bound to the active site cysteine through a thioester bond. This is consistent with the kinetics of the reaction that have shown acetoacetyl-CoA to be a potent inhibitor of the overall reaction, and provides a starting point in the search for a small molecule inhibitor.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16245942}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16245942 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16245942}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Vartia, A A.]] | | [[Category: Vartia, A A.]] |
| | [[Category: Thiolase family]] | | [[Category: Thiolase family]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:44:23 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:08:39 2008'' |
Revision as of 14:08, 28 July 2008
Template:STRUCTURE 1x9e
Crystal structure of HMG-CoA synthase from Enterococcus faecalis
Template:ABSTRACT PUBMED 16245942
About this Structure
1X9E is a Single protein structure of sequence from Enterococcus faecalis. Full crystallographic information is available from OCA.
Reference
X-ray crystal structures of HMG-CoA synthase from Enterococcus faecalis and a complex with its second substrate/inhibitor acetoacetyl-CoA., Steussy CN, Vartia AA, Burgner JW 2nd, Sutherlin A, Rodwell VW, Stauffacher CV, Biochemistry. 2005 Nov 1;44(43):14256-67. PMID:16245942
Page seeded by OCA on Mon Jul 28 17:08:39 2008
