1zow
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Crystal Structure of S. aureus FabH, beta-ketoacyl carrier protein synthase III
OverviewOverview
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.
About this StructureAbout this Structure
1ZOW is a Single protein structure of sequence from Staphylococcus aureus. Active as Beta-ketoacyl-acyl-carrier-protein synthase I, with EC number 2.3.1.41 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure and substrate specificity of the beta-ketoacyl-acyl carrier protein synthase III (FabH) from Staphylococcus aureus., Qiu X, Choudhry AE, Janson CA, Grooms M, Daines RA, Lonsdale JT, Khandekar SS, Protein Sci. 2005 Aug;14(8):2087-94. Epub 2005 Jun 29. PMID:15987898
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