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8QPP

Bacillus subtilis MutS2-collided disome complex (stalled 70S)

This is a non-PDB format compatible entry.
Summary for 8QPP
Entry DOI10.2210/pdb8qpp/pdb
EMDB information18558
Descriptor50S ribosomal protein L32, 30S ribosomal protein S5, 30S ribosomal protein S6, ... (53 entities in total)
Functional Keywordsmuts2, collision, disome, splitting, quality control, ribosome
Biological sourceBacillus subtilis
More
Total number of polymer chains53
Total formula weight2234257.16
Authors
Park, E.,Mackens-Kiani, T.,Berhane, R.,Esser, H.,Erdenebat, C.,Burroughs, A.M.,Berninghausen, O.,Aravind, L.,Beckmann, R.,Green, R.,Buskirk, A.R. (deposition date: 2023-10-02, release date: 2023-12-27, Last modification date: 2024-10-23)
Primary citationPark, E.N.,Mackens-Kiani, T.,Berhane, R.,Esser, H.,Erdenebat, C.,Burroughs, A.M.,Berninghausen, O.,Aravind, L.,Beckmann, R.,Green, R.,Buskirk, A.R.
B. subtilis MutS2 splits stalled ribosomes into subunits without mRNA cleavage.
Embo J., 43:484-506, 2024
Cited by
PubMed Abstract: Stalled ribosomes are rescued by pathways that recycle the ribosome and target the nascent polypeptide for degradation. In E. coli, these pathways are triggered by ribosome collisions through the recruitment of SmrB, a nuclease that cleaves the mRNA. In B. subtilis, the related protein MutS2 was recently implicated in ribosome rescue. Here we show that MutS2 is recruited to collisions by its SMR and KOW domains, and we reveal the interaction of these domains with collided ribosomes by cryo-EM. Using a combination of in vivo and in vitro approaches, we show that MutS2 uses its ABC ATPase activity to split ribosomes, targeting the nascent peptide for degradation through the ribosome quality control pathway. However, unlike SmrB, which cleaves mRNA in E. coli, we see no evidence that MutS2 mediates mRNA cleavage or promotes ribosome rescue by tmRNA. These findings clarify the biochemical and cellular roles of MutS2 in ribosome rescue in B. subtilis and raise questions about how these pathways function differently in diverse bacteria.
PubMed: 38177497
DOI: 10.1038/s44318-023-00010-3
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.4 Å)
Structure validation

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