6EMF
Crystal structure of Rrp1 from Chaetomium thermophilum in space group C2
Summary for 6EMF
Entry DOI | 10.2210/pdb6emf/pdb |
Related | 6ELZ 6EM1 6EM3 6EM4 6EM5 |
EMDB information | 3889 3890 3891 3892 3893 |
Descriptor | G0S4M2, 1,2-ETHANEDIOL, PROLINE, ... (4 entities in total) |
Functional Keywords | ribosome biogenesis, ribosome, translation |
Biological source | Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) |
Total number of polymer chains | 2 |
Total formula weight | 66867.94 |
Authors | Ahmed, Y.L.,Sinning, I. (deposition date: 2017-10-02, release date: 2017-12-27, Last modification date: 2024-05-08) |
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 | X-RAY DIFFRACTION (2.65 Å) |
Structure validation
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