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Title | Structure of the GTP Form of Elongation Factor 4 (EF4) Bound to the Ribosome. |
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Journal, issue, pages | J Biol Chem, Vol. 291, Issue 25, Page 12943-12950, Year 2016 |
Publish date | Jun 17, 2016 |
Authors | Veerendra Kumar / Rya Ero / Tofayel Ahmed / Kwok Jian Goh / Yin Zhan / Shashi Bhushan / Yong-Gui Gao / |
PubMed Abstract | Elongation factor 4 (EF4) is a member of the family of ribosome-dependent translational GTPase factors, along with elongation factor G and BPI-inducible protein A. Although EF4 is highly conserved in ...Elongation factor 4 (EF4) is a member of the family of ribosome-dependent translational GTPase factors, along with elongation factor G and BPI-inducible protein A. Although EF4 is highly conserved in bacterial, mitochondrial, and chloroplast genomes, its exact biological function remains controversial. Here we present the cryo-EM reconstitution of the GTP form of EF4 bound to the ribosome with P and E site tRNAs at 3.8-Å resolution. Interestingly, our structure reveals an unrotated ribosome rather than a clockwise-rotated ribosome, as observed in the presence of EF4-GDP and P site tRNA. In addition, we also observed a counterclockwise-rotated form of the above complex at 5.7-Å resolution. Taken together, our results shed light on the interactions formed between EF4, the ribosome, and the P site tRNA and illuminate the GTPase activation mechanism at previously unresolved detail. |
External links | J Biol Chem / PubMed:27137929 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.8 - 5.9 Å |
Structure data | |
Chemicals | ChemComp-GCP: |
Source |
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Keywords | RIBOSOME / EF4/LepA / translational GTPase factors / translocation / reverse |