4V7P
Recognition of the amber stop codon by release factor RF1.
This is a non-PDB format compatible entry.
Summary for 4V7P
| Entry DOI | 10.2210/pdb4v7p/pdb |
| Related | 1zbt 3D5A 3F1E 3MRZ 3MS0 3MS1 |
| Descriptor | 16S rRNA (1504-MER), 30S ribosomal protein S10, 30S ribosomal protein S11, ... (58 entities in total) |
| Functional Keywords | 70s, ribosome, termination, release factor, rf1, amber, stop codon, uag |
| Biological source | Thermus thermophilus More |
| Cellular location | Cytoplasm : Q72HB8 |
| Total number of polymer chains | 110 |
| Total formula weight | 4434764.15 |
| Authors | Korostelev, A.,Zhu, J.,Asahara, H.,Noller, H.F. (deposition date: 2010-04-29, release date: 2014-07-09, Last modification date: 2023-09-20) |
| Primary citation | Korostelev, A.,Zhu, J.,Asahara, H.,Noller, H.F. Recognition of the amber UAG stop codon by release factor RF1. Embo J., 29:2577-2585, 2010 Cited by PubMed Abstract: We report the crystal structure of a termination complex containing release factor RF1 bound to the 70S ribosome in response to an amber (UAG) codon at 3.6-A resolution. The amber codon is recognized in the 30S subunit-decoding centre directly by conserved elements of domain 2 of RF1, including T186 of the PVT motif. Together with earlier structures, the mechanisms of recognition of all three stop codons by release factors RF1 and RF2 can now be described. Our structure confirms that the backbone amide of Q230 of the universally conserved GGQ motif is positioned to contribute directly to the catalysis of the peptidyl-tRNA hydrolysis reaction through stabilization of the leaving group and/or transition state. We also observe synthetic-negative interactions between mutations in the switch loop of RF1 and in helix 69 of 23S rRNA, revealing that these structural features interact functionally in the termination process. These findings are consistent with our proposal that structural rearrangements of RF1 and RF2 are critical to accurate translation termination. PubMed: 20588254DOI: 10.1038/emboj.2010.139 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.62 Å) |
Structure validation
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