3IL9

Structure of E. coli FabH

Summary for 3IL9

• Entry DOI: 10.2210/pdb3il9/pdb
• Related: 3IL3 3IL4 3IL5 3IL6 3IL7
• Descriptor: 3-oxoacyl-[acyl-carrier-protein] synthase 3 (2 entities in total)
• Functional Keywords: fabh, fatty acid biosynthesis, antibiotic, acyltransferase, lipid synthesis, multifunctional enzyme, transferase
• Biological source: Escherichia coli K-12
• Cellular location: Cytoplasm : P0A6R0
• Total number of polymer chains: 2
• Total formula weight: 72717.85

Authors

Gajiwala, K.S.,Margosiak, S.,Lu, J.,Cortez, J.,Su, Y.,Nie, Z.,Appelt, K. (deposition date: 2009-08-06, release date: 2009-08-25, Last modification date: 2024-10-30)

Primary citation

Gajiwala, K.S.,Margosiak, S.,Lu, J.,Cortez, J.,Su, Y.,Nie, Z.,Appelt, K.
Crystal structures of bacterial FabH suggest a molecular basis for the substrate specificity of the enzyme.
Febs Lett., 583:2939-2946, 2009

PubMed Abstract: FabH (beta-ketoacyl-acyl carrier protein synthase III) is unique in that it initiates fatty acid biosynthesis, is inhibited by long-chain fatty acids providing means for feedback control of the process, and dictates the fatty acid profile of the organism by virtue of its substrate specificity. We report the crystal structures of bacterial FabH enzymes from four different pathogenic species: Enterococcus faecalis, Haemophilus influenzae, Staphylococcus aureus and Escherichia coli. Structural data on the enzyme from different species show important differences in the architecture of the substrate-binding sites that parallel the inter-species diversity in the substrate specificities of these enzymes.

PubMed: 19665020
DOI: 10.1016/j.febslet.2009.08.001

Experimental method

X-RAY DIFFRACTION (1.85 Å)