3HNZ
Structure of E. coli FabF(C163A) in Complex with Platensimycin
Summary for 3HNZ
| Entry DOI | 10.2210/pdb3hnz/pdb |
| Related | 3HO2 3HO9 |
| Descriptor | 3-oxoacyl-[acyl-carrier-protein] synthase 2, PLATENSIMYCIN (3 entities in total) |
| Functional Keywords | platensimycin analog, fabf, ketoacyl synthase, acyltransferase, fatty acid biosynthesis, lipid synthesis, transferase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 45046.71 |
| Authors | Soisson, S.M.,Parthasarathy, G. (deposition date: 2009-06-01, release date: 2010-02-09, Last modification date: 2024-02-21) |
| Primary citation | Singh, S.B.,Ondeyka, J.G.,Herath, K.B.,Zhang, C.,Jayasuriya, H.,Zink, D.L.,Parthasarathy, G.,Becker, J.W.,Wang, J.,Soisson, S.M. Isolation, enzyme-bound structure and antibacterial activity of platencin A1 from Streptomyces platensis. Bioorg.Med.Chem.Lett., 19:4756-4759, 2009 Cited by PubMed Abstract: Natural products continue to serve as one of the best sources for discovery of antibacterial agents as exemplified by the recent discoveries of platensimycin and platencin. Chemical modifications as well as discovery of congeners are the main sources for gaining knowledge of structure-activity relationship of natural products. Screening for congeners in the extracts of the fermentation broths of Streptomyces platensis led to the isolation of platencin A(1), a hydroxy congener of platencin. The hydroxylation of the tricyclic enone moiety negatively affected the antibacterial activity and appears to be consistent with the hydrophobic binding pocket of the FabF. Isolation, structure, enzyme-bound structure and activity of platencin A(1) and two other congeners have been described. PubMed: 19581087DOI: 10.1016/j.bmcl.2009.06.061 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.75 Å) |
Structure validation
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