8JIV
Atomic structure of wheat ribosome reveals unique features of the plant ribosomes
This is a non-PDB format compatible entry.
Summary for 8JIV
| Entry DOI | 10.2210/pdb8jiv/pdb |
| EMDB information | 36331 |
| Descriptor | 25S rRNA, 60S ribosomal protein L7a, Ribosomal protein L6 alpha-beta domain-containing protein, ... (47 entities in total) |
| Functional Keywords | protein synthesis machinery, eukaryotic ribosome, plant, translation, ribosome |
| Biological source | Triticum aestivum (bread wheat) More |
| Total number of polymer chains | 44 |
| Total formula weight | 1984466.28 |
| Authors | Mishra, R.K.,Sharma, P.,Hussain, T. (deposition date: 2023-05-28, release date: 2024-03-27, Last modification date: 2024-05-22) |
| Primary citation | Mishra, R.K.,Sharma, P.,Khaja, F.T.,Uday, A.B.,Hussain, T. Cryo-EM structure of wheat ribosome reveals unique features of the plant ribosomes. Structure, 32:562-, 2024 Cited by PubMed Abstract: Plants being sessile organisms exhibit unique features in ribosomes, which might aid in rapid gene expression and regulation in response to varying environmental conditions. Here, we present high-resolution structures of the 60S and 80S ribosomes from wheat, a monocot staple crop plant (Triticum aestivum). While plant ribosomes have unique plant-specific rRNA modification (Cm1847) in the peptide exit tunnel (PET), the zinc-finger motif in eL34 is absent, and uL4 is extended, making an exclusive interaction network. We note differences in the eL15-helix 11 (25S) interaction, eL6-ES7 assembly, and certain rRNA chemical modifications between monocot and dicot ribosomes. In eukaryotes, we observe highly conserved rRNA modification (Gm75) in 5.8S rRNA and a flipped base (G1506) in PET. These features are likely involved in sensing or stabilizing nascent chain. Finally, we discuss the importance of the universal conservation of three consecutive rRNA modifications in all ribosomes for their interaction with A-site aminoacyl-tRNA. PubMed: 38458197DOI: 10.1016/j.str.2024.02.006 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.84 Å) |
Structure validation
Download full validation report
