4G5G
ef-tu (Escherichia coli) complexed with nvp-ldu796
Summary for 4G5G
| Entry DOI | 10.2210/pdb4g5g/pdb |
| Related PRD ID | PRD_000901 |
| Descriptor | Elongation factor Tu 1, thiomuracin A derivative, MAGNESIUM ION, ... (6 entities in total) |
| Functional Keywords | elongation factor, translation-antibiotic complex, translation/antibiotic |
| Biological source | Escherichia coli More |
| Cellular location | Cytoplasm: P0CE47 |
| Total number of polymer chains | 2 |
| Total formula weight | 45288.88 |
| Authors | Palestrant, D. (deposition date: 2012-07-17, release date: 2012-12-26, Last modification date: 2023-11-15) |
| Primary citation | LaMarche, M.J.,Leeds, J.A.,Dzink-Fox, J.,Gangl, E.,Krastel, P.,Neckermann, G.,Palestrant, D.,Patane, M.A.,Rann, E.M.,Tiamfook, S.,Yu, D. Antibiotic optimization and chemical structure stabilization of thiomuracin A. J.Med.Chem., 55:6934-6941, 2012 Cited by PubMed Abstract: Synthetic studies of the antimicrobial secondary metabolite thiomuracin A (1) were initiated to improve chemical stability and physicochemical properties. Functional group modifications of 1 included removing the C2-C7 side chain, derivatizing the C84 epoxide region, and altering the C44 hydroxyphenylalanine motif. The resulting derivatives simplified and stabilized the chemical structure and were evaluated for antibacterial activity relative to 1. The simplified structure and improved organic solubility of the derivatives facilitated isolation yields from fermentation broths and simplified the procedures involved for the process. These advancements increased material supply for continued medicinal chemistry optimization and culminated in the identification of 2, a structurally simplified and chemically stable analogue of 1 which retained potent antibiotic activity. PubMed: 22812377DOI: 10.1021/jm300783c PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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