3I56
Co-crystal structure of Triacetyloleandomcyin Bound to the Large Ribosomal Subunit
Summary for 3I56
| Entry DOI | 10.2210/pdb3i56/pdb |
| Related | 3I55 |
| Descriptor | 50S ribosomal protein L2P, 50S ribosomal protein L13P, 50S ribosomal protein L14P, ... (39 entities in total) |
| Functional Keywords | large ribosomal subunit, triacetyloleandomcyin, ribonucleoprotein, ribosomal protein, rna-binding, rrna-binding, trna-binding, metal-binding, zinc, zinc-finger, acetylation, ribosome, ribosome-antibiotic complex, ribosome/antibiotic |
| Biological source | Haloarcula marismortui (Halobacterium marismortui) More |
| Cellular location | Cytoplasm : P12743 |
| Total number of polymer chains | 31 |
| Total formula weight | 1493373.87 |
| Authors | Gurel, G.,Blaha, G.,Steitz, T.A.,Moore, P.B. (deposition date: 2009-07-03, release date: 2010-03-09, Last modification date: 2024-02-21) |
| Primary citation | Gurel, G.,Blaha, G.,Steitz, T.A.,Moore, P.B. Structures of triacetyloleandomycin and mycalamide A bind to the large ribosomal subunit of Haloarcula marismortui. Antimicrob.Agents Chemother., 53:5010-5014, 2009 Cited by PubMed Abstract: Structures have been obtained for the complexes that triacetyloleandomycin and mycalamide A form with the large ribosomal subunit of Haloarcula marismortui. Triacetyloleandomycin binds in the nascent peptide tunnel and inhibits the activity of ribosomes by blocking the growth of the nascent peptide chain. Mycalamide A binds to the E site and inhibits protein synthesis by occupying the space normally occupied by the CCA end of E-site-bound tRNAs. PubMed: 19738021DOI: 10.1128/AAC.00817-09 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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