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TitleRibosome-induced changes in elongation factor Tu conformation control GTP hydrolysis.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 106, Issue 4, Page 1063-1068, Year 2009
Publish dateJan 27, 2009
AuthorsElizabeth Villa / Jayati Sengupta / Leonardo G Trabuco / Jamie LeBarron / William T Baxter / Tanvir R Shaikh / Robert A Grassucci / Poul Nissen / Måns Ehrenberg / Klaus Schulten / Joachim Frank /
PubMed AbstractIn translation, elongation factor Tu (EF-Tu) molecules deliver aminoacyl-tRNAs to the mRNA-programmed ribosome. The GTPase activity of EF-Tu is triggered by ribosome-induced conformational changes of ...In translation, elongation factor Tu (EF-Tu) molecules deliver aminoacyl-tRNAs to the mRNA-programmed ribosome. The GTPase activity of EF-Tu is triggered by ribosome-induced conformational changes of the factor that play a pivotal role in the selection of the cognate aminoacyl-tRNAs. We present a 6.7-A cryo-electron microscopy map of the aminoacyl-tRNA x EF-Tu x GDP x kirromycin-bound Escherichia coli ribosome, together with an atomic model of the complex obtained through molecular dynamics flexible fitting. The model reveals the conformational changes in the conserved GTPase switch regions of EF-Tu that trigger hydrolysis of GTP, along with key interactions, including those between the sarcin-ricin loop and the P loop of EF-Tu, and between the effector loop of EF-Tu and a conserved region of the 16S rRNA. Our data suggest that GTP hydrolysis on EF-Tu is controlled through a hydrophobic gate mechanism.
External linksProc Natl Acad Sci U S A / PubMed:19122150 / PubMed Central
MethodsEM (single particle)
Resolution6.7 Å
Structure data

5036

4v69

EMDB-5036: Aminoacyl-tRNA-EF-Tu-GDP-kir ternary complex-bound E. coli 70S ribosome
PDB-4v69: Ternary complex-bound E.coli 70S ribosome.
Method: EM (single particle) / Resolution: 6.7 Å

Chemicals

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

Source
  • escherichia coli (E. coli)
KeywordsRIBOSOME / ternary complex / flexible fitting / cryo-EM / 30S / 50S / tRNA / mRNA / EF-Tu / 70S / Ribonucleoprotein / Ribosomal protein / RNA-binding / rRNA-binding / Antibiotic resistance / Repressor / Transcription / Transcription regulation / Transcription termination / Translation regulation / tRNA-binding / Methylation / Endonuclease / Hydrolase / Nuclease / Cell membrane / Elongation factor / GTP-binding / Membrane / Nucleotide-binding / Phosphoprotein / Protein biosynthesis

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