4W2E
Crystal structure of Elongation Factor 4 (EF4/LepA) bound to the Thermus thermophilus 70S ribosome
This is a non-PDB format compatible entry.
Summary for 4W2E
| Entry DOI | 10.2210/pdb4w2e/pdb |
| Descriptor | 23S Ribosomal RNA, 50S ribosomal protein L13, 50S ribosomal protein L14, ... (62 entities in total) |
| Functional Keywords | ef4, lepa, translation, elogation, acylated p-site trna, ribosome |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 57 |
| Total formula weight | 2339375.44 |
| Authors | Gagnon, M.G.,Lin, J.,Steitz, T.A. (deposition date: 2014-06-04, release date: 2014-10-01, Last modification date: 2024-11-06) |
| Primary citation | Gagnon, M.G.,Lin, J.,Bulkley, D.,Steitz, T.A. Crystal structure of elongation factor 4 bound to a clockwise ratcheted ribosome. Science, 345:684-687, 2014 Cited by PubMed Abstract: Elongation factor 4 (EF4/LepA) is a highly conserved guanosine triphosphatase translation factor. It was shown to promote back-translocation of tRNAs on posttranslocational ribosome complexes and to compete with elongation factor G for interaction with pretranslocational ribosomes, inhibiting the elongation phase of protein synthesis. Here, we report a crystal structure of EF4-guanosine diphosphate bound to the Thermus thermophilus ribosome with a P-site tRNA at 2.9 angstroms resolution. The C-terminal domain of EF4 reaches into the peptidyl transferase center and interacts with the acceptor stem of the peptidyl-tRNA in the P site. The ribosome is in an unusual state of ratcheting with the 30S subunit rotated clockwise relative to the 50S subunit, resulting in a remodeled decoding center. The structure is consistent with EF4 functioning either as a back-translocase or a ribosome sequester. PubMed: 25104389DOI: 10.1126/science.1253525 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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