4V5A
Structure of the Ribosome Recycling Factor bound to the Thermus thermophilus 70S ribosome with mRNA, ASL-Phe and tRNA-fMet
This is a non-PDB format compatible entry.
Summary for 4V5A
| Entry DOI | 10.2210/pdb4v5a/pdb |
| Related | 1FJG 1GIX 1I94 1I95 1I96 1I97 1IBK 1IBL 1IBM 1J5E 1JGO 1JGP 1JGQ 1L1U 1N32 1N33 1N34 1N36 1PNS 1PNX 1XMO 1XMQ 1XNQ 1XNR 1YL4 2B64 2B9M 2B9O 2F4V 2J00 2J02 2UU9 2UUA 2UUB 2UUC 2UXB 2UXC |
| Descriptor | 16S ribosomal RNA, 30S RIBOSOMAL PROTEIN S10, 30S RIBOSOMAL PROTEIN S11, ... (58 entities in total) |
| Functional Keywords | ribosomal protein, ribonucleoprotein, trna-binding, rrna-binding, metal-binding, rrf, trna, mrna, ribosome, recycling, protein biosynthesis, rna-binding, zinc-finger, translation |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 112 |
| Total formula weight | 4489984.99 |
| Authors | Weixlbaumer, A.,Petry, S.,Dunham, C.M.,Selmer, M.,Kelley, A.C.,Ramakrishnan, V. (deposition date: 2007-06-28, release date: 2014-07-09, Last modification date: 2024-01-10) |
| Primary citation | Weixlbaumer, A.,Petry, S.,Dunham, C.M.,Selmer, M.,Kelley, A.C.,Ramakrishnan, V. Crystal structure of the ribosome recycling factor bound to the ribosome. Nat. Struct. Mol. Biol., 14:733-737, 2007 Cited by PubMed Abstract: In bacteria, disassembly of the ribosome at the end of translation is facilitated by an essential protein factor termed ribosome recycling factor (RRF), which works in concert with elongation factor G. Here we describe the crystal structure of the Thermus thermophilus RRF bound to a 70S ribosomal complex containing a stop codon in the A site, a transfer RNA anticodon stem-loop in the P site and tRNA(fMet) in the E site. The work demonstrates that structures of translation factors bound to 70S ribosomes can be determined at reasonably high resolution. Contrary to earlier reports, we did not observe any RRF-induced changes in bridges connecting the two subunits. This suggests that such changes are not a direct requirement for or consequence of RRF binding but possibly arise from the subsequent stabilization of a hybrid state of the ribosome. PubMed: 17660830DOI: 10.1038/nsmb1282 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.5 Å) |
Structure validation
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