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7UG6

Cryo-EM structure of pre-60S ribosomal subunit, unmethylated G2922

This is a non-PDB format compatible entry.
Summary for 7UG6
Entry DOI10.2210/pdb7ug6/pdb
EMDB information26485
Descriptor25S rRNA, 60S ribosomal protein L7-A, 60S ribosomal protein L8-A, ... (54 entities in total)
Functional Keywordsribosome, ribosome biogenesis, rrna modification, methylation
Biological sourceSaccharomyces cerevisiae S288C
More
Total number of polymer chains52
Total formula weight2338390.00
Authors
Yelland, J.N.,Bravo, J.P.K.,Black, J.J.B.,Taylor, D.W.,Johnson, A.W. (deposition date: 2022-03-24, release date: 2022-12-21, Last modification date: 2024-06-12)
Primary citationYelland, J.N.,Bravo, J.P.K.,Black, J.J.,Taylor, D.W.,Johnson, A.W.
A single 2'-O-methylation of ribosomal RNA gates assembly of a functional ribosome.
Nat.Struct.Mol.Biol., 30:91-98, 2023
Cited by
PubMed Abstract: RNA modifications are widespread in biology and abundant in ribosomal RNA. However, the importance of these modifications is not well understood. We show that methylation of a single nucleotide, in the catalytic center of the large subunit, gates ribosome assembly. Massively parallel mutational scanning of the essential nuclear GTPase Nog2 identified important interactions with rRNA, particularly with the 2'-O-methylated A-site base Gm2922. We found that methylation of G2922 is needed for assembly and efficient nuclear export of the large subunit. Critically, we identified single amino acid changes in Nog2 that completely bypass dependence on G2922 methylation and used cryoelectron microscopy to directly visualize how methylation flips Gm2922 into the active site channel of Nog2. This work demonstrates that a single RNA modification is a critical checkpoint in ribosome biogenesis, suggesting that such modifications can play an important role in regulation and assembly of macromolecular machines.
PubMed: 36536102
DOI: 10.1038/s41594-022-00891-8
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.9 Å)
Structure validation

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