4MJR
E. coli sliding clamp in complex with (S)-Carprofen
Summary for 4MJR
| Entry DOI | 10.2210/pdb4mjr/pdb |
| Related | 4MJP 4MJQ |
| Descriptor | DNA polymerase III subunit beta, TRIETHYLENE GLYCOL, DI(HYDROXYETHYL)ETHER, ... (7 entities in total) |
| Functional Keywords | poliii beta, sliding clamp, dnan, transferase-transferase inhibitor complex, transferase/transferase inhibitor |
| Biological source | Escherichia coli |
| Cellular location | Cytoplasm: P0A988 |
| Total number of polymer chains | 2 |
| Total formula weight | 82405.99 |
| Authors | Yin, Z.,Oakley, A.J. (deposition date: 2013-09-04, release date: 2013-09-18, Last modification date: 2023-09-20) |
| Primary citation | Yin, Z.,Wang, Y.,Whittell, L.R.,Jergic, S.,Liu, M.,Harry, E.,Dixon, N.E.,Kelso, M.J.,Beck, J.L.,Oakley, A.J. DNA replication is the target for the antibacterial effects of nonsteroidal anti-inflammatory drugs. Chem.Biol., 21:481-487, 2014 Cited by PubMed Abstract: Evidence suggests that some nonsteroidal anti-inflammatory drugs (NSAIDs) possess antibacterial properties with an unknown mechanism. We describe the in vitro antibacterial properties of the NSAIDs carprofen, bromfenac, and vedaprofen, and show that these NSAIDs inhibit the Escherichia coli DNA polymerase III β subunit, an essential interaction hub that acts as a mobile tether on DNA for many essential partner proteins in DNA replication and repair. Crystal structures show that the three NSAIDs bind to the sliding clamp at a common binding site required for partner binding. Inhibition of interaction of the clamp loader and/or the replicative polymerase α subunit with the sliding clamp is demonstrated using an in vitro DNA replication assay. NSAIDs thus present promising lead scaffolds for novel antibacterial agents targeting the sliding clamp. PubMed: 24631121DOI: 10.1016/j.chembiol.2014.02.009 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.62 Å) |
Structure validation
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