8PVK
Chaetomium thermophilum pre-60S State 5 - pre-5S rotation - L1 inward - composite structure
This is a non-PDB format compatible entry.
Summary for 8PVK
| Entry DOI | 10.2210/pdb8pvk/pdb |
| EMDB information | 17903 17904 17905 17906 17907 17969 |
| Descriptor | 26S rRNA, Ribosome biogenesis protein NSA2 homolog, Putative GTP binding protein, ... (63 entities in total) |
| Functional Keywords | biogenesis, pre-60s, 5s rnp, ribosome |
| Biological source | Thermochaetoides thermophila DSM 1495 More |
| Total number of polymer chains | 60 |
| Total formula weight | 3088184.76 |
| Authors | Thoms, M.,Cheng, J.,Denk, T.,Berninghausen, O.,Beckmann, R. (deposition date: 2023-07-17, release date: 2023-12-06, Last modification date: 2023-12-20) |
| Primary citation | Thoms, M.,Lau, B.,Cheng, J.,Fromm, L.,Denk, T.,Kellner, N.,Flemming, D.,Fischer, P.,Falquet, L.,Berninghausen, O.,Beckmann, R.,Hurt, E. Structural insights into coordinating 5S RNP rotation with ITS2 pre-RNA processing during ribosome formation. Embo Rep., 24:e57984-e57984, 2023 Cited by PubMed Abstract: The rixosome defined in Schizosaccharomyces pombe and humans performs diverse roles in pre-ribosomal RNA processing and gene silencing. Here, we isolate and describe the conserved rixosome from Chaetomium thermophilum, which consists of two sub-modules, the sphere-like Rix1-Ipi3-Ipi1 and the butterfly-like Las1-Grc3 complex, connected by a flexible linker. The Rix1 complex of the rixosome utilizes Sda1 as landing platform on nucleoplasmic pre-60S particles to wedge between the 5S rRNA tip and L1-stalk, thereby facilitating the 180° rotation of the immature 5S RNP towards its mature conformation. Upon rixosome positioning, the other sub-module with Las1 endonuclease and Grc3 polynucleotide-kinase can reach a strategic position at the pre-60S foot to cleave and 5' phosphorylate the nearby ITS2 pre-rRNA. Finally, inward movement of the L1 stalk permits the flexible Nop53 N-terminus with its AIM motif to become positioned at the base of the L1-stalk to facilitate Mtr4 helicase-exosome participation for completing ITS2 removal. Thus, the rixosome structure elucidates the coordination of two central ribosome biogenesis events, but its role in gene silencing may adapt similar strategies. PubMed: 37921038DOI: 10.15252/embr.202357984 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.55 Å) |
Structure validation
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