6UCQ

Crystal structure of the Thermus thermophilus 70S ribosome recycling complex

This is a non-PDB format compatible entry.

Summary for 6UCQ

• Entry DOI: 10.2210/pdb6ucq/pdb
• Descriptor: 23S Ribosomal RNA, 50S ribosomal protein L15, 50S ribosomal protein L16, ... (60 entities in total)
• Functional Keywords: recycling, ef-g, rrf, 70s ribosome, p/r trna, ribosomal protein ul5, ribosome
• Biological source: Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579); More
• Total number of polymer chains: 112
• Total formula weight: 4699418.07

Authors

Zhou, D.,Tanzawa, T.,Gagnon, M.G.,Lin, J. (deposition date: 2019-09-17, release date: 2019-12-25, Last modification date: 2025-03-19)

Primary citation

Zhou, D.,Tanzawa, T.,Lin, J.,Gagnon, M.G.
Structural basis for ribosome recycling by RRF and tRNA.
Nat.Struct.Mol.Biol., 27:25-32, 2020

PubMed Abstract: The bacterial ribosome is recycled into subunits by two conserved proteins, elongation factor G (EF-G) and the ribosome recycling factor (RRF). The molecular basis for ribosome recycling by RRF and EF-G remains unclear. Here, we report the crystal structure of a posttermination Thermus thermophilus 70S ribosome complexed with EF-G, RRF and two transfer RNAs at a resolution of 3.5 Å. The deacylated tRNA in the peptidyl (P) site moves into a previously unsuspected state of binding (peptidyl/recycling, p/R) that is analogous to that seen during initiation. The terminal end of the p/R-tRNA forms nonfavorable contacts with the 50S subunit while RRF wedges next to central inter-subunit bridges, illuminating the active roles of tRNA and RRF in dissociation of ribosomal subunits. The structure uncovers a missing snapshot of tRNA as it transits between the P and exit (E) sites, providing insights into the mechanisms of ribosome recycling and tRNA translocation.

PubMed: 31873307
DOI: 10.1038/s41594-019-0350-7

Experimental method

X-RAY DIFFRACTION (3.5 Å)