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6M62

Cryo-Em structure of eukaryotic pre-60S ribosome subunit from Saccharomyces cerevisiae rpf2 delta 255-344 strain, C4 state.

This is a non-PDB format compatible entry.
Summary for 6M62
Entry DOI10.2210/pdb6m62/pdb
EMDB information30108
DescriptorRDN25-1 rRNA, 60S ribosomal protein L5, 60S ribosomal protein L6-A, ... (61 entities in total)
Functional Keywordspre-60s, rpf2, ribosome
Biological sourceSaccharomyces cerevisiae S288C
More
Total number of polymer chains58
Total formula weight2669354.05
Authors
Li, Y.,Micic, J. (deposition date: 2020-03-12, release date: 2020-08-26, Last modification date: 2024-10-16)
Primary citationMicic, J.,Li, Y.,Wu, S.,Wilson, D.,Tutuncuoglu, B.,Gao, N.,Woolford Jr., J.L.
Coupling of 5S RNP rotation with maturation of functional centers during large ribosomal subunit assembly.
Nat Commun, 11:3751-3751, 2020
Cited by
PubMed Abstract: The protein composition and structure of assembling 60S ribosomal subunits undergo numerous changes as pre-ribosomes transition from the nucleolus to the nucleoplasm. This includes stable anchoring of the Rpf2 subcomplex containing 5S rRNA, rpL5, rpL11, Rpf2 and Rrs1, which initially docks onto the flexible domain V of rRNA at earlier stages of assembly. In this work, we tested the function of the C-terminal domain (CTD) of Rpf2 during these anchoring steps, by truncating this extension and assaying effects on middle stages of subunit maturation. The rpf2Δ255-344 mutation affects proper folding of rRNA helices H68-70 during anchoring of the Rpf2 subcomplex. In addition, several assembly factors (AFs) are absent from pre-ribosomes or in altered conformations. Consequently, major remodeling events fail to occur: rotation of the 5S RNP, maturation of the peptidyl transferase center (PTC) and the nascent polypeptide exit tunnel (NPET), and export of assembling subunits to the cytoplasm.
PubMed: 32719344
DOI: 10.1038/s41467-020-17534-5
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.2 Å)
Structure validation

226707

数据于2024-10-30公开中

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