6BOH

Antibiotic blasticidin S and E. coli release factor 1 (containing deletion 302-304) bound to the 70S ribosome

This is a non-PDB format compatible entry.

Summary for 6BOH

• Entry DOI: 10.2210/pdb6boh/pdb
• Descriptor: 16S ribosomal RNA, 50S ribosomal protein L9, 50S ribosomal protein L13, ... (58 entities in total)
• Functional Keywords: class i release factors, closed rf1, stop-codon recognition, termination accuracy, blasticidin s, ribosome-antibiotic complex, ribosome/antibiotic
• Biological source: Escherichia coli; More
• Total number of polymer chains: 114
• Total formula weight: 4622553.74

Authors

Svidritskiy, E.,Korostelev, A.A. (deposition date: 2017-11-20, release date: 2018-05-23, Last modification date: 2025-03-19)

Primary citation

Svidritskiy, E.,Korostelev, A.A.
Conformational Control of Translation Termination on the 70S Ribosome.
Structure, 26:821-, 2018

PubMed Abstract: Translation termination ensures proper lengths of cellular proteins. During termination, release factor (RF) recognizes a stop codon and catalyzes peptide release. Conformational changes in RF are thought to underlie accurate translation termination. However, structural studies of ribosome termination complexes have only captured RFs in a conformation that is consistent with the catalytically active state. Here, we employ a hyper-accurate RF1 variant to obtain crystal structures of 70S termination complexes that suggest a structural pathway for RF1 activation. We trapped RF1 conformations with the catalytic domain outside of the peptidyl-transferase center, while the codon-recognition domain binds the stop codon. Stop-codon recognition induces 30S decoding-center rearrangements that precede accommodation of the catalytic domain. The separation of codon recognition from the opening of the catalytic domain suggests how rearrangements in RF1 and in the ribosomal decoding center coordinate stop-codon recognition with peptide release, ensuring accurate translation termination.

PubMed: 29731232
DOI: 10.1016/j.str.2018.04.001

Experimental method

X-RAY DIFFRACTION (3.4 Å)