5MDY
Structure of ArfA and TtRF2 bound to the 70S ribosome (pre-accommodated state)
This is a non-PDB format compatible entry.
Summary for 5MDY
Entry DOI | 10.2210/pdb5mdy/pdb |
EMDB information | 3492 |
Descriptor | 23S ribosomal RNA, 50S ribosomal protein L4, 50S ribosomal protein L5, ... (62 entities in total) |
Functional Keywords | ribosome, arfa, rf2, trans-translation, 70s, 50s, 30s, rescue termination, cryo-em |
Biological source | Escherichia coli K-12 More |
Total number of polymer chains | 58 |
Total formula weight | 2262715.70 |
Authors | James, N.R.,Brown, A.,Gordiyenko, Y.,Ramakrishnan, V. (deposition date: 2016-11-13, release date: 2016-12-21, Last modification date: 2024-04-24) |
Primary citation | James, N.R.,Brown, A.,Gordiyenko, Y.,Ramakrishnan, V. Translational termination without a stop codon. Science, 354:1437-1440, 2016 Cited by PubMed Abstract: Ribosomes stall when they encounter the end of messenger RNA (mRNA) without an in-frame stop codon. In bacteria, these "nonstop" complexes can be rescued by alternative ribosome-rescue factor A (ArfA). We used electron cryomicroscopy to determine structures of ArfA bound to the ribosome with 3'-truncated mRNA, at resolutions ranging from 3.0 to 3.4 angstroms. ArfA binds within the ribosomal mRNA channel and substitutes for the absent stop codon in the A site by specifically recruiting release factor 2 (RF2), initially in a compact preaccommodated state. A similar conformation of RF2 may occur on stop codons, suggesting a general mechanism for release-factor-mediated translational termination in which a conformational switch leads to peptide release only when the appropriate signal is present in the A site. PubMed: 27934701DOI: 10.1126/science.aai9127 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.35 Å) |
Structure validation
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