Summary for 5VPP
| Entry DOI | 10.2210/pdb5vpp/pdb |
| Related | 5VPO |
| Descriptor | 23S rRNA, 50S ribosomal protein L14, 50S ribosomal protein L15, ... (55 entities in total) |
| Functional Keywords | frameshift, ribosome, suppressor mutants, trnas, translation |
| Biological source | Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) More |
| Total number of polymer chains | 106 |
| Total formula weight | 4425145.75 |
| Authors | Hong, S.,Sunita, S.,Dunkle, J.A.,Maehigashi, T.,Dunham, C.M. (deposition date: 2017-05-05, release date: 2018-09-26, Last modification date: 2024-12-25) |
| Primary citation | Hong, S.,Sunita, S.,Maehigashi, T.,Hoffer, E.D.,Dunkle, J.A.,Dunham, C.M. Mechanism of tRNA-mediated +1 ribosomal frameshifting. Proc. Natl. Acad. Sci. U.S.A., 115:11226-11231, 2018 Cited by PubMed Abstract: Accurate translation of the genetic code is critical to ensure expression of proteins with correct amino acid sequences. Certain tRNAs can cause a shift out of frame (i.e., frameshifting) due to imbalances in tRNA concentrations, lack of tRNA modifications or insertions or deletions in tRNAs (called frameshift suppressors). Here, we determined the structural basis for how frameshift-suppressor tRNA (a derivative of tRNA) reprograms the mRNA frame to translate a 4-nt codon when bound to the bacterial ribosome. After decoding at the aminoacyl (A) site, the crystal structure of the anticodon stem-loop of tRNA bound in the peptidyl (P) site reveals ASL conformational changes that allow for recoding into the +1 mRNA frame. Furthermore, a crystal structure of full-length tRNA programmed in the P site shows extensive conformational rearrangements of the 30S head and body domains similar to what is observed in a translocation intermediate state containing elongation factor G (EF-G). The 30S movement positions tRNA toward the 30S exit (E) site disrupting key 16S rRNA-mRNA interactions that typically define the mRNA frame. In summary, this tRNA-induced 30S domain change in the absence of EF-G causes the ribosome to lose its grip on the mRNA and uncouples the canonical forward movement of the tRNAs during elongation. PubMed: 30262649DOI: 10.1073/pnas.1809319115 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.9 Å) |
Structure validation
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