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6EMF

Crystal structure of Rrp1 from Chaetomium thermophilum in space group C2

Summary for 6EMF
Entry DOI10.2210/pdb6emf/pdb
Related6ELZ 6EM1 6EM3 6EM4 6EM5
EMDB information3889 3890 3891 3892 3893
DescriptorG0S4M2, 1,2-ETHANEDIOL, PROLINE, ... (4 entities in total)
Functional Keywordsribosome biogenesis, ribosome, translation
Biological sourceChaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
Total number of polymer chains2
Total formula weight66867.94
Authors
Ahmed, Y.L.,Sinning, I. (deposition date: 2017-10-02, release date: 2017-12-27, Last modification date: 2024-05-08)
Primary citationKater, 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: 29245012
DOI: 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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