7qgn

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Structure of the SmrB-bound E. coli disome - stalled 70S ribosomeStructure of the SmrB-bound E. coli disome - stalled 70S ribosome

Structural highlights

7qgn is a 10 chain structure with sequence from Escherichia coli and Vibrio alginolyticus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 3.37Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

Ribosome rescue pathways recycle stalled ribosomes and target problematic mRNAs and aborted proteins for degradation(1,2). In bacteria, it remains unclear how rescue pathways distinguish ribosomes stalled in the middle of a transcript from actively translating ribosomes(3-6). Here, using a genetic screen in Escherichia coli, we discovered a new rescue factor that has endonuclease activity. SmrB cleaves mRNAs upstream of stalled ribosomes, allowing the ribosome rescue factor tmRNA (which acts on truncated mRNAs(3)) to rescue upstream ribosomes. SmrB is recruited to ribosomes and is activated by collisions. Cryo-electron microscopy structures of collided disomes from E. coli and Bacillus subtilis show distinct and conserved arrangements of individual ribosomes and the composite SmrB-binding site. These findings reveal the underlying mechanisms by which ribosome collisions trigger ribosome rescue in bacteria.

Ribosome collisions induce mRNA cleavage and ribosome rescue in bacteria.,Saito K, Kratzat H, Campbell A, Buschauer R, Burroughs AM, Berninghausen O, Aravind L, Green R, Beckmann R, Buskirk AR Nature. 2022 Mar;603(7901):503-508. doi: 10.1038/s41586-022-04416-7. Epub 2022 , Mar 9. PMID:35264790[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Saito K, Kratzat H, Campbell A, Buschauer R, Burroughs AM, Berninghausen O, Aravind L, Green R, Beckmann R, Buskirk AR. Ribosome collisions induce mRNA cleavage and ribosome rescue in bacteria. Nature. 2022 Mar;603(7901):503-508. PMID:35264790 doi:10.1038/s41586-022-04416-7

7qgn, resolution 3.37Å

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OCA