8UU5

Cryo-EM structure of the Listeria innocua 70S ribosome (head-swiveled) in complex with pe/E-tRNA (structure I-B)

This is a non-PDB format compatible entry.

Summary for 8UU5

• Entry DOI: 10.2210/pdb8uu5/pdb
• EMDB information: 42557
• Descriptor: 16S Ribosomal RNA, Small ribosomal subunit protein uS10, Small ribosomal subunit protein uS11, ... (54 entities in total)
• Functional Keywords: cryo-em, recycling, time-resolved, ribosome
• Biological source: Escherichia coli; More
• Total number of polymer chains: 51
• Total formula weight: 2156361.91

Authors

Seely, S.M.,Basu, R.S.,Gagnon, M.G. (deposition date: 2023-10-31, release date: 2024-02-28, Last modification date: 2024-05-01)

Primary citation

Seely, S.M.,Basu, R.S.,Gagnon, M.G.
Mechanistic insights into the alternative ribosome recycling by HflXr.
Nucleic Acids Res., 52:4053-4066, 2024

PubMed Abstract: During stress conditions such as heat shock and antibiotic exposure, ribosomes stall on messenger RNAs, leading to inhibition of protein synthesis. To remobilize ribosomes, bacteria use rescue factors such as HflXr, a homolog of the conserved housekeeping GTPase HflX that catalyzes the dissociation of translationally inactive ribosomes into individual subunits. Here we use time-resolved cryo-electron microscopy to elucidate the mechanism of ribosome recycling by Listeria monocytogenes HflXr. Within the 70S ribosome, HflXr displaces helix H69 of the 50S subunit and induces long-range movements of the platform domain of the 30S subunit, disrupting inter-subunit bridges B2b, B2c, B4, B7a and B7b. Our findings unveil a unique ribosome recycling strategy by HflXr which is distinct from that mediated by RRF and EF-G. The resemblance between HflXr and housekeeping HflX suggests that the alternative ribosome recycling mechanism reported here is universal in the prokaryotic kingdom.

PubMed: 38407413
DOI: 10.1093/nar/gkae128

Experimental method

ELECTRON MICROSCOPY (3 Å)