6TB3
yeast 80S ribosome in complex with the Not5 subunit of the CCR4-NOT complex
This is a non-PDB format compatible entry.
Summary for 6TB3
| Entry DOI | 10.2210/pdb6tb3/pdb |
| EMDB information | 10431 |
| Descriptor | Saccharomyces cerevisiae S288C 18S ribosomal RNA (RDN18-1), rRNA, 40S ribosomal protein S6-A, 40S ribosomal protein S7-A, ... (86 entities in total) |
| Functional Keywords | not5, ccr4-not complex, translation control, translation |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) More |
| Total number of polymer chains | 83 |
| Total formula weight | 3041158.64 |
| Authors | Buschauer, R.,Cheng, J.,Berninghausen, O.,Tesina, P.,Becker, T.,Beckmann, R. (deposition date: 2019-10-31, release date: 2020-04-22, Last modification date: 2024-05-22) |
| Primary citation | Buschauer, R.,Matsuo, Y.,Sugiyama, T.,Chen, Y.H.,Alhusaini, N.,Sweet, T.,Ikeuchi, K.,Cheng, J.,Matsuki, Y.,Nobuta, R.,Gilmozzi, A.,Berninghausen, O.,Tesina, P.,Becker, T.,Coller, J.,Inada, T.,Beckmann, R. The Ccr4-Not complex monitors the translating ribosome for codon optimality. Science, 368:-, 2020 Cited by PubMed Abstract: Control of messenger RNA (mRNA) decay rate is intimately connected to translation elongation, but the spatial coordination of these events is poorly understood. The Ccr4-Not complex initiates mRNA decay through deadenylation and activation of decapping. We used a combination of cryo-electron microscopy, ribosome profiling, and mRNA stability assays to examine the recruitment of Ccr4-Not to the ribosome via specific interaction of the Not5 subunit with the ribosomal E-site in This interaction occurred when the ribosome lacked accommodated A-site transfer RNA, indicative of low codon optimality. Loss of the interaction resulted in the inability of the mRNA degradation machinery to sense codon optimality. Our findings elucidate a physical link between the Ccr4-Not complex and the ribosome and provide mechanistic insight into the coupling of decoding efficiency with mRNA stability. PubMed: 32299921DOI: 10.1126/science.aay6912 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.8 Å) |
Structure validation
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