4V9K
70S ribosome translocation intermediate GDPNP-I containing elongation factor EFG/GDPNP, mRNA, and tRNA bound in the pe*/E state.
This is a non-PDB format compatible entry.
Summary for 4V9K
| Entry DOI | 10.2210/pdb4v9k/pdb |
| Related PRD ID | PRD_000226 |
| Descriptor | 30S ribosomal protein S2, 30S ribosomal protein S11, 30S ribosomal protein S12, ... (62 entities in total) |
| Functional Keywords | gdpnp, chimeric hybrid state ribosome, ribosome, translocation intermediate, ef-g, mrna, trna, ribosome-antibiotic complex, ribosome/antibiotic |
| Biological source | Thermus thermophilus More |
| Cellular location | Cytoplasm : Q72I01 |
| Total number of polymer chains | 122 |
| Total formula weight | 4569712.81 |
| Authors | Zhou, J.,Lancaster, L.,Donohue, J.P.,Noller, H.F. (deposition date: 2013-04-24, release date: 2014-07-09, Last modification date: 2023-12-06) |
| Primary citation | Zhou, J.,Lancaster, L.,Donohue, J.P.,Noller, H.F. Crystal structures of EF-G-ribosome complexes trapped in intermediate states of translocation. Science, 340:1236086-1236086, 2013 Cited by PubMed Abstract: Translocation of messenger and transfer RNA (mRNA and tRNA) through the ribosome is a crucial step in protein synthesis, whose mechanism is not yet understood. The crystal structures of three Thermus ribosome-tRNA-mRNA-EF-G complexes trapped with β,γ-imidoguanosine 5'-triphosphate (GDPNP) or fusidic acid reveal conformational changes occurring during intermediate states of translocation, including large-scale rotation of the 30S subunit head and body. In all complexes, the tRNA acceptor ends occupy the 50S subunit E site, while their anticodon stem loops move with the head of the 30S subunit to positions between the P and E sites, forming chimeric intermediate states. Two universally conserved bases of 16S ribosomal RNA that intercalate between bases of the mRNA may act as "pawls" of a translocational ratchet. These findings provide new insights into the molecular mechanism of ribosomal translocation. PubMed: 23812722DOI: 10.1126/science.1236086 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.5 Å) |
Structure validation
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