Journal
EMBO JOURNAL
Volume 28, Issue 6, Pages 755-765Publisher
WILEY
DOI: 10.1038/emboj.2009.26
Keywords
cryo-electron microscopy; elongation factor; GTPase; ribosome; translation
Categories
Funding
- DFG [SFB 740 TP A3, TP Z1, SP 1130/2-1]
- VolkswagenStiftung
- European Union [3D-EM]
- Senatsverwaltung fur Wissenschaft
- Forschung und Kultur Berlin (UltraStructureNetwork, Anwenderzentrum)
- US NIH [GM 60635, GM 67624]
- Medical Research Council (UK)
- Wellcome Trust
- Agouron Institute
- Louis-Jeantet foundation
- Medical Research Council [MC_U105184332] Funding Source: researchfish
- MRC [MC_U105184332] Funding Source: UKRI
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We have used single-particle reconstruction in cryo-electron microscopy to determine a structure of the Thermus thermophilus ribosome in which the ternary complex of elongation factor Tu (EF-Tu), tRNA and guanine nucleotide has been trapped on the ribosome using the antibiotic kirromycin. This represents the state in the decoding process just after codon recognition by tRNA and the resulting GTP hydrolysis by EF-Tu, but before the release of EF-Tu from the ribosome. Progress in sample purification and image processing made it possible to reach a resolution of 6.4A. Secondary structure elements in tRNA, EF-Tu and the ribosome, and even GDP and kirromycin, could all be visualized directly. The structure reveals a complex conformational rearrangement of the tRNA in the A/T state and the interactions with the functionally important switch regions of EF-Tu crucial to GTP hydrolysis. Thus, the structure provides insights into the molecular mechanism of signalling codon recognition from the decoding centre of the 30S subunit to the GTPase centre of EF-Tu.
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