5J8B
Crystal structure of Elongation Factor 4 (EF-4/LepA) in complex with GDPCP bound to the Thermus thermophilus 70S ribosome
This is a non-PDB format compatible entry.
Summary for 5J8B
| Entry DOI | 10.2210/pdb5j8b/pdb |
| Related | 5J4B 5J4C |
| Descriptor | 23S Ribosomal RNA, 50S ribosomal protein L11, 50S ribosomal protein L13, ... (64 entities in total) |
| Functional Keywords | 70s, ribosome, ef-4, lepa, translation, elongation, trna |
| Biological source | Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) More |
| Total number of polymer chains | 59 |
| Total formula weight | 2391370.27 |
| Authors | Gagnon, M.G.,Lin, J.,Steitz, T.A. (deposition date: 2016-04-07, release date: 2016-05-25, Last modification date: 2024-03-06) |
| Primary citation | Gagnon, M.G.,Lin, J.,Steitz, T.A. Elongation factor 4 remodels the A-site tRNA on the ribosome. Proc.Natl.Acad.Sci.USA, 113:4994-4999, 2016 Cited by PubMed Abstract: During translation, a plethora of protein factors bind to the ribosome and regulate protein synthesis. Many of those factors are guanosine triphosphatases (GTPases), proteins that catalyze the hydrolysis of guanosine 5'-triphosphate (GTP) to promote conformational changes. Despite numerous studies, the function of elongation factor 4 (EF-4/LepA), a highly conserved translational GTPase, has remained elusive. Here, we present the crystal structure at 2.6-Å resolution of the Thermus thermophilus 70S ribosome bound to EF-4 with a nonhydrolyzable GTP analog and A-, P-, and E-site tRNAs. The structure reveals the interactions of EF-4 with the A-site tRNA, including contacts between the C-terminal domain (CTD) of EF-4 and the acceptor helical stem of the tRNA. Remarkably, EF-4 induces a distortion of the A-site tRNA, allowing it to interact simultaneously with EF-4 and the decoding center of the ribosome. The structure provides insights into the tRNA-remodeling function of EF-4 on the ribosome and suggests that the displacement of the CCA-end of the A-site tRNA away from the peptidyl transferase center (PTC) is functionally significant. PubMed: 27092003DOI: 10.1073/pnas.1522932113 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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