6YLE
Rix1-Rea1 pre-60S particle - Rix1-subcomplex, body 3 (rigid body refinement)
Summary for 6YLE
| Entry DOI | 10.2210/pdb6yle/pdb |
| EMDB information | 10836 |
| Descriptor | Pre-rRNA-processing protein IPI3, Pre-rRNA-processing protein RIX1, Pre-rRNA-processing protein IPI1 (3 entities in total) |
| Functional Keywords | pre-60s, biogenesis, lsu, large subunit, ribosome assembly, ribosome |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) More |
| Total number of polymer chains | 5 |
| Total formula weight | 335281.97 |
| Authors | Kater, L.,Beckmann, R. (deposition date: 2020-04-07, release date: 2020-07-29, Last modification date: 2024-05-22) |
| Primary citation | Kater, L.,Mitterer, V.,Thoms, M.,Cheng, J.,Berninghausen, O.,Beckmann, R.,Hurt, E. Construction of the Central Protuberance and L1 Stalk during 60S Subunit Biogenesis. Mol.Cell, 79:615-628.e5, 2020 Cited by PubMed Abstract: Ribosome assembly is driven by numerous assembly factors, including the Rix1 complex and the AAA ATPase Rea1. These two assembly factors catalyze 60S maturation at two distinct states, triggering poorly understood large-scale structural transitions that we analyzed by cryo-electron microscopy. Two nuclear pre-60S intermediates were discovered that represent previously unknown states after Rea1-mediated removal of the Ytm1-Erb1 complex and reveal how the L1 stalk develops from a pre-mature nucleolar to a mature-like nucleoplasmic state. A later pre-60S intermediate shows how the central protuberance arises, assisted by the nearby Rix1-Rea1 machinery, which was solved in its pre-ribosomal context to molecular resolution. This revealed a Rix1-Ipi3 tetramer anchored to the pre-60S via Ipi1, strategically positioned to monitor this decisive remodeling. These results are consistent with a general underlying principle that temporarily stabilized immature RNA domains are successively remodeled by assembly factors, thereby ensuring failsafe assembly progression. PubMed: 32668200DOI: 10.1016/j.molcel.2020.06.032 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
Download full validation report
