6OSQ

RF1 accommodated state bound Release complex 70S at long incubation time point

This is a non-PDB format compatible entry.

Summary for 6OSQ

• Entry DOI: 10.2210/pdb6osq/pdb
• EMDB information: 20187
• Descriptor: 23S ribosomal RNA, 50S ribosomal protein L6, 50S ribosomal protein L9, ... (57 entities in total)
• Functional Keywords: time-resolved cryo-em, termination, short-lived, millisecond, ribosome
• Biological source: Escherichia coli; More
• Total number of polymer chains: 55
• Total formula weight: 2181010.53

Authors

Fu, Z.,Indrisiunaite, G.,Kaledhonkar, S.,Shah, B.,Sun, M.,Chen, B.,Grassucci, R.A.,Ehrenberg, M.,Frank, J. (deposition date: 2019-05-02, release date: 2019-06-26, Last modification date: 2020-01-08)

Primary citation

Fu, Z.,Indrisiunaite, G.,Kaledhonkar, S.,Shah, B.,Sun, M.,Chen, B.,Grassucci, R.A.,Ehrenberg, M.,Frank, J.
The structural basis for release-factor activation during translation termination revealed by time-resolved cryogenic electron microscopy.
Nat Commun, 10:2579-2579, 2019

PubMed Abstract: When the ribosome encounters a stop codon, it recruits a release factor (RF) to hydrolyze the ester bond between the peptide chain and tRNA. RFs have structural motifs that recognize stop codons in the decoding center and a GGQ motif for induction of hydrolysis in the peptidyl transfer center 70 Å away. Surprisingly, free RF2 is compact, with only 20 Å between its codon-reading and GGQ motifs. Cryo-EM showed that ribosome-bound RFs have extended structures, suggesting that RFs are compact when entering the ribosome and then extend their structures upon stop codon recognition. Here we use time-resolved cryo-EM to visualize transient compact forms of RF1 and RF2 at 3.5 and 4 Å resolution, respectively, in the codon-recognizing ribosome complex on the native pathway. About 25% of complexes have RFs in the compact state at 24 ms reaction time, and within 60 ms virtually all ribosome-bound RFs are transformed to their extended forms.

PubMed: 31189921
DOI: 10.1038/s41467-019-10608-z

Experimental method

ELECTRON MICROSCOPY (3.5 Å)