6ELZ
State E (TAP-Flag-Ytm1 E80A) - Visualizing the assembly pathway of nucleolar pre-60S ribosomes
This is a non-PDB format compatible entry.
Summary for 6ELZ
Entry DOI | 10.2210/pdb6elz/pdb |
Related | 6ELZ |
EMDB information | 3891 |
Descriptor | 25S ribosomal RNA, 60S ribosomal protein L22-A, 60S ribosomal protein L27-A, ... (55 entities in total) |
Functional Keywords | large subunit biogenesis nucleolus, ribosome |
Biological source | Saccharomyces cerevisiae S288c (Baker's yeast) More |
Total number of polymer chains | 54 |
Total formula weight | 2788714.70 |
Authors | Kater, L.,Cheng, J.,Barrio-Garcia, C.,Hurt, E.,Beckmann, R. (deposition date: 2017-09-30, release date: 2017-12-27, Last modification date: 2024-10-23) |
Primary citation | Kater, L.,Thoms, M.,Barrio-Garcia, C.,Cheng, J.,Ismail, S.,Ahmed, Y.L.,Bange, G.,Kressler, D.,Berninghausen, O.,Sinning, I.,Hurt, E.,Beckmann, R. Visualizing the Assembly Pathway of Nucleolar Pre-60S Ribosomes. Cell, 171:1599-1610.e14, 2017 Cited by PubMed Abstract: Eukaryotic 60S ribosomal subunits are comprised of three rRNAs and ∼50 ribosomal proteins. The initial steps of their formation take place in the nucleolus, but, owing to a lack of structural information, this process is poorly understood. Using cryo-EM, we solved structures of early 60S biogenesis intermediates at 3.3 Å to 4.5 Å resolution, thereby providing insights into their sequential folding and assembly pathway. Besides revealing distinct immature rRNA conformations, we map 25 assembly factors in six different assembly states. Notably, the Nsa1-Rrp1-Rpf1-Mak16 module stabilizes the solvent side of the 60S subunit, and the Erb1-Ytm1-Nop7 complex organizes and connects through Erb1's meandering N-terminal extension, eight assembly factors, three ribosomal proteins, and three 25S rRNA domains. Our structural snapshots reveal the order of integration and compaction of the six major 60S domains within early nucleolar 60S particles developing stepwise from the solvent side around the exit tunnel to the central protuberance. PubMed: 29245012DOI: 10.1016/j.cell.2017.11.039 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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