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6FT6

Structure of the Nop53 pre-60S particle bound to the exosome nuclear cofactors

This is a non-PDB format compatible entry.
Summary for 6FT6
Entry DOI10.2210/pdb6ft6/pdb
EMDB information4301 4302
Descriptor7S ribosomal RNA, Bud site selection protein 20, 60S ribosomal protein L11-A, ... (60 entities in total)
Functional Keywordsrna exosome, ribosome, pre-ribosome, mtr4, helicase, rna
Biological sourceSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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Total number of polymer chains57
Total formula weight2670685.70
Authors
Schuller, J.M.,Falk, S.,Conti, E. (deposition date: 2018-02-20, release date: 2018-03-28, Last modification date: 2024-11-06)
Primary citationSchuller, J.M.,Falk, S.,Fromm, L.,Hurt, E.,Conti, E.
Structure of the nuclear exosome captured on a maturing preribosome.
Science, 360:219-222, 2018
Cited by
PubMed Abstract: The RNA exosome complex processes and degrades a wide range of transcripts, including ribosomal RNAs (rRNAs). We used cryo-electron microscopy to visualize the yeast nuclear exosome holocomplex captured on a precursor large ribosomal subunit (pre-60) during 7-to-5.8 rRNA processing. The cofactors of the nuclear exosome are sandwiched between the ribonuclease core complex (Exo-10) and the remodeled "foot" structure of the pre-60 particle, which harbors the 5.8 rRNA precursor. The exosome-associated helicase Mtr4 recognizes the preribosomal substrate by docking to specific sites on the 25 rRNA, captures the 3' extension of the 5.8 rRNA, and channels it toward Exo-10. The structure elucidates how the exosome forms a structural and functional unit together with its massive pre-60 substrate to process rRNA during ribosome maturation.
PubMed: 29519915
DOI: 10.1126/science.aar5428
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.9 Å)
Structure validation

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