4V8P
T.thermophila 60S ribosomal subunit in complex with initiation factor 6.
This is a non-PDB format compatible entry.
Summary for 4V8P
| Entry DOI | 10.2210/pdb4v8p/pdb |
| Descriptor | 26S RRNA, UBIQUITIN-60S RIBOSOMAL PROTEIN L40, RPL34, ... (50 entities in total) |
| Functional Keywords | ribosome, eukaryotic initiation factor 6, eif6, 60s, translation, large ribosomal subunit, rrna, ribosomal protein |
| Biological source | TETRAHYMENA THERMOPHILA More |
| Cellular location | Ubiquitin: Cytoplasm . 60S ribosomal protein L40: Cytoplasm : P0DJ25 Cytoplasm : P0DJ19 P0DJ21 P0DJ18 P0DJ24 P0DJ52 O96774 P0DJ55 Q231U7 P0DJ17 Q22X38 Q245F2 |
| Total number of polymer chains | 184 |
| Total formula weight | 7975794.74 |
| Authors | Klinge, S.,Voigts-Hoffmann, F.,Leibundgut, M.,Arpagaus, S.,Ban, N. (deposition date: 2011-09-14, release date: 2014-07-09, Last modification date: 2024-01-10) |
| Primary citation | Klinge, S.,Voigts-Hoffmann, F.,Leibundgut, M.,Arpagaus, S.,Ban, N. Crystal Structure of the Eukaryotic 60S Ribosomal Subunit in Complex with Initiation Factor 6. Science, 334:941-, 2011 Cited by PubMed Abstract: Protein synthesis in all organisms is catalyzed by ribosomes. In comparison to their prokaryotic counterparts, eukaryotic ribosomes are considerably larger and are subject to more complex regulation. The large ribosomal subunit (60S) catalyzes peptide bond formation and contains the nascent polypeptide exit tunnel. We present the structure of the 60S ribosomal subunit from Tetrahymena thermophila in complex with eukaryotic initiation factor 6 (eIF6), cocrystallized with the antibiotic cycloheximide (a eukaryotic-specific inhibitor of protein synthesis), at a resolution of 3.5 angstroms. The structure illustrates the complex functional architecture of the eukaryotic 60S subunit, which comprises an intricate network of interactions between eukaryotic-specific ribosomal protein features and RNA expansion segments. It reveals the roles of eukaryotic ribosomal protein elements in the stabilization of the active site and the extent of eukaryotic-specific differences in other functional regions of the subunit. Furthermore, it elucidates the molecular basis of the interaction with eIF6 and provides a structural framework for further studies of ribosome-associated diseases and the role of the 60S subunit in the initiation of protein synthesis. PubMed: 22052974DOI: 10.1126/SCIENCE.1211204 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.52 Å) |
Structure validation
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