8WKP
Structural basis of translation inhibition by a valine tRNA-derived fragment
This is a non-PDB format compatible entry.
Summary for 8WKP
| Entry DOI | 10.2210/pdb8wkp/pdb |
| EMDB information | 37604 |
| Descriptor | RNA (1328-MER), 30S ribosomal protein S12, 30S ribosomal protein S15, ... (29 entities in total) |
| Functional Keywords | sulfolobus acidocaldarius ribosome, ribosome |
| Biological source | Sulfolobus acidocaldarius DSM 639 More |
| Total number of polymer chains | 28 |
| Total formula weight | 892487.91 |
| Authors | Wang, Y.H.,Zhou, J. (deposition date: 2023-09-28, release date: 2024-04-10, Last modification date: 2024-05-22) |
| Primary citation | Wu, Y.,Ni, M.T.,Wang, Y.H.,Wang, C.,Hou, H.,Zhang, X.,Zhou, J. Structural basis of translation inhibition by a valine tRNA-derived fragment. Life Sci Alliance, 7:-, 2024 Cited by PubMed Abstract: Translational regulation by non-coding RNAs is a mechanism commonly used by cells to fine-tune gene expression. A fragment derived from an archaeal valine tRNA (Val-tRF) has been previously identified to bind the small subunit of the ribosome and inhibit translation in Here, we present three cryo-electron microscopy structures of Val-tRF bound to the small subunit of ribosomes at resolutions between 4.02 and 4.53 Å. Within these complexes, Val-tRF was observed to bind to conserved RNA-interacting sites, including the ribosomal decoding center. The binding of Val-tRF destabilizes helices h24, h44, and h45 and the anti-Shine-Dalgarno sequence of 16S rRNA. The binding position of this molecule partially overlaps with the translation initiation factor aIF1A and occludes the mRNA P-site codon. Moreover, we found that the binding of Val-tRF is associated with steric hindrance of the H69 base of 23S rRNA in the large ribosome subunit, thereby preventing 70S assembly. Our data exemplify how tRNA-derived fragments bind to ribosomes and provide new insights into the mechanisms underlying translation inhibition by Val-tRFs. PubMed: 38599770DOI: 10.26508/lsa.202302488 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.62 Å) |
Structure validation
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