6OGF

70S termination complex with RF2 bound to the UGA codon. Partially rotated ribosome with RF2 bound (Structure III).

This is a non-PDB format compatible entry.

Summary for 6OGF

• Entry DOI: 10.2210/pdb6ogf/pdb
• EMDB information: 20056
• Descriptor: 50S ribosomal protein L2, 50S ribosomal protein L16, 50S ribosomal protein L17, ... (55 entities in total)
• Functional Keywords: ribosome recycling, translation termination, rf2, intersubunit rotation, ribosome
• Biological source: Escherichia coli; More
• Total number of polymer chains: 55
• Total formula weight: 2228594.25

Authors

Svidritskiy, E.,Demo, G.,Loveland, A.B.,Xu, C.,Korostelev, A.A. (deposition date: 2019-04-02, release date: 2019-09-25, Last modification date: 2024-03-20)

Primary citation

Svidritskiy, E.,Demo, G.,Loveland, A.B.,Xu, C.,Korostelev, A.A.
Extensive ribosome and RF2 rearrangements during translation termination.
Elife, 8:-, 2019

PubMed Abstract: Protein synthesis ends when a ribosome reaches an mRNA stop codon. Release factors (RFs) decode the stop codon, hydrolyze peptidyl-tRNA to release the nascent protein, and then dissociate to allow ribosome recycling. To visualize termination by RF2, we resolved a cryo-EM ensemble of 70S•RF2 structures at up to 3.3 Å in a single sample. Five structures suggest a highly dynamic termination pathway. Upon peptidyl-tRNA hydrolysis, the CCA end of deacyl-tRNA departs from the peptidyl transferase center. The catalytic GGQ loop of RF2 is rearranged into a long β-hairpin that plugs the peptide tunnel, biasing a nascent protein toward the ribosome exit. Ribosomal intersubunit rotation destabilizes the catalytic RF2 domain on the 50S subunit and disassembles the central intersubunit bridge B2a, resulting in RF2 departure. Our structures visualize how local rearrangements and spontaneous inter-subunit rotation poise the newly-made protein and RF2 to dissociate in preparation for ribosome recycling.

PubMed: 31513010
DOI: 10.7554/eLife.46850

Experimental method

ELECTRON MICROSCOPY (3.9 Å)