2OTJ
13-deoxytedanolide bound to the large subunit of Haloarcula marismortui
Summary for 2OTJ
| Entry DOI | 10.2210/pdb2otj/pdb |
| Related | 1S72 2OTL |
| Descriptor | 23S ribosomal RNA, 50S ribosomal protein L10e, 50S ribosomal protein L13P, ... (38 entities in total) |
| Functional Keywords | 13 deoxytedanolide, antibiotic complex, 50s, ribosome |
| Biological source | Haloarcula marismortui More |
| Cellular location | Cytoplasm : P12743 |
| Total number of polymer chains | 31 |
| Total formula weight | 1478889.74 |
| Authors | Blaha, G.,Schroeder, S.J.,Tirado-Rives, J. (deposition date: 2007-02-08, release date: 2007-04-03, Last modification date: 2023-08-30) |
| Primary citation | Schroeder, S.J.,Blaha, G.,Tirado-Rives, J.,Steitz, T.A.,Moore, P.B. The Structures of Antibiotics Bound to the E Site Region of the 50 S Ribosomal Subunit of Haloarcula marismortui: 13-Deoxytedanolide and Girodazole. J.Mol.Biol., 367:1471-1479, 2007 Cited by PubMed Abstract: Crystal structures of the 50 S ribosomal subunit from Haloarcula marismortui complexed with two antibiotics have identified new sites at which antibiotics interact with the ribosome and inhibit protein synthesis. 13-Deoxytedanolide binds to the E site of the 50 S subunit at the same location as the CCA of tRNA, and thus appears to inhibit protein synthesis by competing with deacylated tRNAs for E site binding. Girodazole binds near the E site region, but is somewhat buried and may inhibit tRNA binding by interfering with conformational changes that occur at the E site. The specificity of 13-deoxytedanolide for eukaryotic ribosomes is explained by its extensive interactions with protein L44e, which is an E site component of archaeal and eukaryotic ribosomes, but not of eubacterial ribosomes. In addition, protein L28, which is unique to the eubacterial E site, overlaps the site occupied by 13-deoxytedanolide, precluding its binding to eubacterial ribosomes. Girodazole is specific for eukarytes and archaea because it makes interactions with L15 that are not possible in eubacteria. PubMed: 17321546DOI: 10.1016/j.jmb.2007.01.081 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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