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| '''Crystal Structure of S. aureus FabH, beta-ketoacyl carrier protein synthase III'''
| | ===Crystal Structure of S. aureus FabH, beta-ketoacyl carrier protein synthase III=== |
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| ==Overview==
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| beta-Ketoacyl-ACP synthase III (FabH), an essential enzyme for bacterial viability, catalyzes the initiation of fatty acid elongation by condensing malonyl-ACP with acetyl-CoA. We have determined the crystal structure of FabH from Staphylococcus aureus, a Gram-positive human pathogen, to 2 A resolution. Although the overall structure of S. aureus FabH is similar to that of Escherichia coli FabH, the primer binding pocket in S. aureus FabH is significantly larger than that present in E. coli FabH. The structural differences, which agree with kinetic parameters, provide explanation for the observed varying substrate specificity for E. coli and S. aureus FabH. The rank order of activity of S. aureus FabH with various acyl-CoA primers was as follows: isobutyryl- > hexanoyl- > butyryl- > isovaleryl- >> acetyl-CoA. The availability of crystal structure may aid in designing potent, selective inhibitors of S. aureus FabH.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15987898}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15987898 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15987898}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Fabh]] | | [[Category: Fabh]] |
| [[Category: Fatty acid biosynthesis]] | | [[Category: Fatty acid biosynthesis]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:53:32 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:57:04 2008'' |