Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structure of the ribosome with elongation factor G trapped in the pretranslocation state.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 110, Issue 52, Page 20994-20999, Year 2013
Publish date	Dec 24, 2013
Authors	Axel F Brilot / Andrei A Korostelev / Dmitri N Ermolenko / Nikolaus Grigorieff /
PubMed Abstract	During protein synthesis, tRNAs and their associated mRNA codons move sequentially on the ribosome from the A (aminoacyl) site to the P (peptidyl) site to the E (exit) site in a process catalyzed by ...During protein synthesis, tRNAs and their associated mRNA codons move sequentially on the ribosome from the A (aminoacyl) site to the P (peptidyl) site to the E (exit) site in a process catalyzed by a universally conserved ribosome-dependent GTPase [elongation factor G (EF-G) in prokaryotes and elongation factor 2 (EF-2) in eukaryotes]. Although the high-resolution structure of EF-G bound to the posttranslocation ribosome has been determined, the pretranslocation conformation of the ribosome bound with EF-G and A-site tRNA has evaded visualization owing to the transient nature of this state. Here we use electron cryomicroscopy to determine the structure of the 70S ribosome with EF-G, which is trapped in the pretranslocation state using antibiotic viomycin. Comparison with the posttranslocation ribosome shows that the small subunit of the pretranslocation ribosome is rotated by ∼12° relative to the large subunit. Domain IV of EF-G is positioned in the cleft between the body and head of the small subunit outwardly of the A site and contacts the A-site tRNA. Our findings suggest a model in which domain IV of EF-G promotes the translocation of tRNA from the A to the P site as the small ribosome subunit spontaneously rotates back from the hybrid, rotated state into the nonrotated posttranslocation state.
External links	Proc Natl Acad Sci U S A / PubMed:24324137 / PubMed Central
Methods	EM (single particle)
Resolution	5.9 - 7.6 Å
Structure data	EMDB-5796: Structure of the Ribosome with Elongation Factor G Trapped in the Pre-Translocation State Method: EM (single particle) / Resolution: 5.9 Å EMDB-5797: Structure of the Ribosome with Elongation Factor G Trapped in the Pre-Translocation State Method: EM (single particle) / Resolution: 6.2 Å EMDB-5798: Structure of the Ribosome with Elongation Factor G Trapped in the Pre-Translocation State Method: EM (single particle) / Resolution: 7.3 Å 5799 4v7c EMDB-5799: Structure of the Ribosome with Elongation Factor G Trapped in the Pre-Translocation State PDB-4v7c: Structure of the Ribosome with Elongation Factor G Trapped in the Pre-Translocation State (pre-translocation *70StRNA structure) Method: EM (single particle) / Resolution: 7.6 Å 5800 4v7d EMDB-5800: Structure of the Ribosome with Elongation Factor G Trapped in the Pre-Translocation State PDB-4v7d: Structure of the Ribosome with Elongation Factor G Trapped in the Pre-Translocation State (pre-translocation 70StRNAEF-G structure) Method: EM (single particle) / Resolution**: 7.6 Å
Chemicals	ChemComp-ZN: Unknown entry
Source	escherichia coli (E. coli) synthetic construct (others) unidentified (others) streptomyces (bacteria) synthetic (others)
Keywords	TRANSLATION / EF-G / single particle analysis / pre-translocation translation complex / viomycin / TRANSLATION/antibiotic / TRANSLATION-antibiotic complex