1ZOW

Crystal Structure of S. aureus FabH, beta-ketoacyl carrier protein synthase III

Summary for 1ZOW

• Entry DOI: 10.2210/pdb1zow/pdb
• Descriptor: 3-oxoacyl-[acyl-carrier-protein] synthase III (2 entities in total)
• Functional Keywords: fabh, fatty acid biosynthesis, transferase
• Biological source: Staphylococcus aureus subsp. aureus
• Cellular location: Cytoplasm (Probable): Q8NXE2
• Total number of polymer chains: 4
• Total formula weight: 135665.59

Authors

Qiu, X.,Choudhry, A.E.,Janson, C.A.,Grooms, M.,Daines, R.A.,Lonsdale, J.T.,Khandekar, S.S. (deposition date: 2005-05-15, release date: 2005-08-09, Last modification date: 2023-08-23)

Primary citation

Qiu, X.,Choudhry, A.E.,Janson, C.A.,Grooms, M.,Daines, R.A.,Lonsdale, J.T.,Khandekar, S.S.
Crystal structure and substrate specificity of the beta-ketoacyl-acyl carrier protein synthase III (FabH) from Staphylococcus aureus.
Protein Sci., 14:2087-2094, 2005

PubMed Abstract: 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.

PubMed: 15987898
DOI: 10.1110/ps.051501605

Experimental method

X-RAY DIFFRACTION (2 Å)