5BY8
The structure of Rpf2-Rrs1 explains its role in ribosome biogenesis
Summary for 5BY8
| Entry DOI | 10.2210/pdb5by8/pdb |
| Descriptor | Rpf2, Rrs1 (3 entities in total) |
| Functional Keywords | ribosome biogenesis, brix domain, protein-rna interaction, 5s rnp, protein complex, biosynthetic protein |
| Biological source | Emericella nidulans FGSC A4 More |
| Total number of polymer chains | 2 |
| Total formula weight | 35452.75 |
| Authors | Kharde, S.,Calvino, F.R.,Gumiero, A.,Wild, K.,Sinning, I. (deposition date: 2015-06-10, release date: 2015-07-08, Last modification date: 2024-11-06) |
| Primary citation | Kharde, S.,Calvino, F.R.,Gumiero, A.,Wild, K.,Sinning, I. The structure of Rpf2-Rrs1 explains its role in ribosome biogenesis. Nucleic Acids Res., 43:7083-7095, 2015 Cited by PubMed Abstract: The assembly of eukaryotic ribosomes is a hierarchical process involving about 200 biogenesis factors and a series of remodeling steps. The 5S RNP consisting of the 5S rRNA, RpL5 and RpL11 is recruited at an early stage, but has to rearrange during maturation of the pre-60S ribosomal subunit. Rpf2 and Rrs1 have been implicated in 5S RNP biogenesis, but their precise role was unclear. Here, we present the crystal structure of the Rpf2-Rrs1 complex from Aspergillus nidulans at 1.5 Å resolution and describe it as Brix domain of Rpf2 completed by Rrs1 to form two anticodon-binding domains with functionally important tails. Fitting the X-ray structure into the cryo-EM density of a previously described pre-60S particle correlates with biochemical data. The heterodimer forms specific contacts with the 5S rRNA, RpL5 and the biogenesis factor Rsa4. The flexible protein tails of Rpf2-Rrs1 localize to the central protuberance. Two helices in the Rrs1 C-terminal tail occupy a strategic position to block the rotation of 25S rRNA and the 5S RNP. Our data provide a structural model for 5S RNP recruitment to the pre-60S particle and explain why removal of Rpf2-Rrs1 is necessary for rearrangements to drive 60S maturation. PubMed: 26117542DOI: 10.1093/nar/gkv640 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.515 Å) |
Structure validation
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