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TitleGTPase activation of elongation factor EF-Tu by the ribosome during decoding.
Journal, issue, pagesEMBO J, Vol. 28, Issue 6, Page 755-765, Year 2009
Publish dateMar 18, 2009
AuthorsJan-Christian Schuette / Frank V Murphy / Ann C Kelley / John R Weir / Jan Giesebrecht / Sean R Connell / Justus Loerke / Thorsten Mielke / Wei Zhang / Pawel A Penczek / V Ramakrishnan / Christian M T Spahn /
PubMed AbstractWe 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), ...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 6.4 A. 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.
External linksEMBO J / PubMed:19229291 / PubMed Central
MethodsEM (single particle)
Resolution6.4 Å
Structure data

5030

4v68

EMDB-5030: GTPase activation of elongation factor EF-Tu by the ribosome during decoding: a cryo-EM structure of the Thermus thermophilus ribosome in which the ternary complex of EF-Tu, tRNA and guanine nucleotide has been trapped on the ribosome with the antibiotic kirromycin.
PDB-4v68: T. thermophilus 70S ribosome in complex with mRNA, tRNAs and EF-Tu.GDP.kirromycin ternary complex, fitted to a 6.4 A Cryo-EM map.
Method: EM (single particle) / Resolution: 6.4 Å

Chemicals

ChemComp-PHA:
PHENYLALANINAL

ChemComp-GDP:
GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM

ChemComp-MAU:
N-METHYL KIRROMYCIN / antibiotic*YM

ChemComp-BME:
BETA-MERCAPTOETHANOL

Source
  • thermus thermophilus (bacteria)
KeywordsRIBOSOME / cryo-electron microscopy/elongation factor/GTPase/ribosome/translation / Ribonucleoprotein / Ribosomal protein / RNA-binding / rRNA-binding / Metal-binding / Zinc-finger / tRNA-binding / Elongation factor / GTP-binding / Nucleotide-binding / Phosphoprotein / Protein biosynthesis

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