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6YLF

Rix1-Rea1 pre-60S particle - Rea1, body 3 (rigid body refinement, composite structure of Rea1 ring and tail)

This is a non-PDB format compatible entry.
Summary for 6YLF
Entry DOI10.2210/pdb6ylf/pdb
EMDB information10837
DescriptorMidasin, Ribosome assembly protein 4 (2 entities in total)
Functional Keywordspre-60s, biogenesis, lsu, large subunit, ribosome assembly, ribosome
Biological sourceSaccharomyces cerevisiae (Baker's yeast)
More
Total number of polymer chains2
Total formula weight617058.22
Authors
Kater, L.,Beckmann, R. (deposition date: 2020-04-07, release date: 2020-07-29, Last modification date: 2024-05-22)
Primary citationKater, 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: 32668200
DOI: 10.1016/j.molcel.2020.06.032
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.2 Å)
Structure validation

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