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7ZUX

Collided ribosome in a disome unit from S. cerevisiae

This is a non-PDB format compatible entry.
Summary for 7ZUX
Entry DOI10.2210/pdb7zux/pdb
Related7ZPQ 7ZRS 7ZS5 7ZUW
EMDB information14979
Descriptor18S ribosomal RNA, 40S ribosomal protein S3, 40S ribosomal protein S4-A, ... (82 entities in total)
Functional Keywordscollision, splitting, rqc, rqt, ribosome
Biological sourceSaccharomyces cerevisiae (baker's yeast)
More
Total number of polymer chains80
Total formula weight3082354.72
Authors
Best, K.M.,Ikeuchi, K.,Kater, L.,Best, D.M.,Musial, J.,Matsuo, Y.,Berninghausen, O.,Becker, T.,Inada, T.,Beckmann, R. (deposition date: 2022-05-13, release date: 2023-02-22, Last modification date: 2024-07-24)
Primary citationBest, K.,Ikeuchi, K.,Kater, L.,Best, D.,Musial, J.,Matsuo, Y.,Berninghausen, O.,Becker, T.,Inada, T.,Beckmann, R.
Structural basis for clearing of ribosome collisions by the RQT complex.
Nat Commun, 14:921-921, 2023
Cited by
PubMed Abstract: Translation of aberrant messenger RNAs can cause stalling of ribosomes resulting in ribosomal collisions. Collided ribosomes are specifically recognized to initiate stress responses and quality control pathways. Ribosome-associated quality control facilitates the degradation of incomplete translation products and requires dissociation of the stalled ribosomes. A central event is therefore the splitting of collided ribosomes by the ribosome quality control trigger complex, RQT, by an unknown mechanism. Here we show that RQT requires accessible mRNA and the presence of a neighboring ribosome. Cryogenic electron microscopy of RQT-ribosome complexes reveals that RQT engages the 40S subunit of the lead ribosome and can switch between two conformations. We propose that the Ski2-like helicase 1 (Slh1) subunit of RQT applies a pulling force on the mRNA, causing destabilizing conformational changes of the small ribosomal subunit, ultimately resulting in subunit dissociation. Our findings provide conceptual framework for a helicase-driven ribosomal splitting mechanism.
PubMed: 36801861
DOI: 10.1038/s41467-023-36230-8
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.5 Å)
Structure validation

226707

건을2024-10-30부터공개중

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