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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 DOI10.2210/pdb5mdy/pdb
EMDB information3492
Descriptor23S ribosomal RNA, 50S ribosomal protein L4, 50S ribosomal protein L5, ... (62 entities in total)
Functional Keywordsribosome, arfa, rf2, trans-translation, 70s, 50s, 30s, rescue termination, cryo-em
Biological sourceEscherichia coli K-12
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Total number of polymer chains58
Total formula weight2262715.70
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 citationJames, 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: 27934701
DOI: 10.1126/science.aai9127
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.35 Å)
Structure validation

226707

数据于2024-10-30公开中

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