3G0Y

Structure of E. coli FabF(C163Q) in complex with dihydroplatensimycin

Summary for 3G0Y

• Entry DOI: 10.2210/pdb3g0y/pdb
• Related: 2GFX
• Descriptor: 3-oxoacyl-[acyl-carrier-protein] synthase 2, 3-({3-[(1S,4aS,6S,7S,9S,9aR)-1,6-dimethyl-2-oxodecahydro-6,9-epoxy-4a,7-methanobenzo[7]annulen-1-yl]propanoyl}amino)-2,4-dihydroxybenzoic acid (3 entities in total)
• Functional Keywords: ketoacyl synthase, antibiotic, acyltransferase, fatty acid biosynthesis, lipid synthesis, transferase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 45105.78

Authors

Soisson, S.M.,Parthasarathy, G. (deposition date: 2009-01-29, release date: 2009-03-17, Last modification date: 2023-09-06)

Primary citation

Shen, H.C.,Ding, F.X.,Singh, S.B.,Parthasarathy, G.,Soisson, S.M.,Ha, S.N.,Chen, X.,Kodali, S.,Wang, J.,Dorso, K.,Tata, J.R.,Hammond, M.L.,Maccoss, M.,Colletti, S.L.
Synthesis and biological evaluation of platensimycin analogs.
Bioorg.Med.Chem.Lett., 19:1623-1627, 2009

PubMed Abstract: Platensimycin (1) displays antibacterial activity due to its inhibition of the elongation condensing enzyme (FabF), a novel mode of action that could potentially lead to a breakthrough in developing a new generation of antibiotics. The medicinal chemistry efforts were focused on the modification of the enone moiety of platensimycin and several analogs showed significant activity against FabF and possess antibacterial activity.

PubMed: 19233644
DOI: 10.1016/j.bmcl.2009.02.006

Experimental method

X-RAY DIFFRACTION (2.6 Å)