3CC4
Co-crystal Structure of Anisomycin Bound to the 50S Ribosomal Subunit
Summary for 3CC4
| Entry DOI | 10.2210/pdb3cc4/pdb |
| Related | 1K73 3CC2 3CC7 3CCE 3CCJ 3CCL 3CCM 3CCQ 3CCR 3CCS 3CCU 3CCV 3CD6 |
| Descriptor | 50S ribosomal protein L2P, 50S ribosomal protein L13P, 50S ribosomal protein L14P, ... (39 entities in total) |
| Functional Keywords | wild type, large ribosomal subunit, haloarcula marismortui, co-crystal, anisomycin, ribosome |
| Biological source | Haloarcula marismortui (Halobacterium marismortui) More |
| Cellular location | Cytoplasm : P12743 |
| Total number of polymer chains | 31 |
| Total formula weight | 1493530.17 |
| Authors | |
| Primary citation | Blaha, G.,Gurel, G.,Schroeder, S.J.,Moore, P.B.,Steitz, T.A. Mutations outside the anisomycin-binding site can make ribosomes drug-resistant. J.Mol.Biol., 379:505-519, 2008 Cited by PubMed Abstract: Eleven mutations that make Haloarcula marismortui resistant to anisomycin, an antibiotic that competes with the amino acid side chains of aminoacyl tRNAs for binding to the A-site cleft of the large ribosomal unit, have been identified in 23S rRNA. The correlation observed between the sensitivity of H. marismortui to anisomycin and the affinity of its large ribosomal subunits for the drug indicates that its response to anisomycin is determined primarily by the binding of the drug to its large ribosomal subunit. The structures of large ribosomal subunits containing resistance mutations show that these mutations can be divided into two classes: (1) those that interfere with specific drug-ribosome interactions and (2) those that stabilize the apo conformation of the A-site cleft of the ribosome relative to its drug-bound conformation. The conformational effects of some mutations of the second kind propagate through the ribosome for considerable distances and are reversed when A-site substrates bind to the ribosome. PubMed: 18455733DOI: 10.1016/j.jmb.2008.03.075 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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