6NTA
Modified ASL proline bound to Thermus thermophilus 70S (cognate)
This is a non-PDB format compatible entry.
Summary for 6NTA
| Entry DOI | 10.2210/pdb6nta/pdb |
| Descriptor | 16S rRNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (57 entities in total) |
| Functional Keywords | ribosome, proline, rna, asl |
| Biological source | Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) More |
| Total number of polymer chains | 108 |
| Total formula weight | 4392615.73 |
| Authors | Hoffer, E.D.,Maehigashi, T.,Subaramanian, S.,Hong, S.,Dunham, C.M. (deposition date: 2019-01-28, release date: 2020-10-14, Last modification date: 2023-10-11) |
| Primary citation | Hoffer, E.,Hong, S.,Sunita, S.,Maehigashi, T.,Gonzalez Jnr, R.L.,Whitford, P.,Dunham, C.M. Structural insights into mRNA reading frame regulation by tRNA modification and slippery codon-anticodon pairing. Elife, 9:-, 2020 Cited by PubMed Abstract: Modifications in the tRNA anticodon loop, adjacent to the three-nucleotide anticodon, influence translation fidelity by stabilizing the tRNA to allow for accurate reading of the mRNA genetic code. One example is the N1-methylguanosine modification at guanine nucleotide 37 (mG37) located in the anticodon loop andimmediately adjacent to the anticodon nucleotides 34, 35, 36. The absence of mG37 in tRNA causes +1 frameshifting on polynucleotide, slippery codons. Here, we report structures of the bacterial ribosome containing tRNA bound to either cognate or slippery codons to determine how the mG37 modification prevents mRNA frameshifting. The structures reveal that certain codon-anticodon contexts and the lack of mG37 destabilize interactions of tRNA with the P site of the ribosome, causing large conformational changes typically only seen during EF-G-mediated translocation of the mRNA-tRNA pairs. These studies provide molecular insights into how mG37 stabilizes the interactions of tRNA with the ribosome in the context of a slippery mRNA codon. PubMed: 33016876DOI: 10.7554/eLife.51898 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
Download full validation report
