Format

Send to

Choose Destination
J Biol Chem. 2016 Jun 17;291(25):12943-50. doi: 10.1074/jbc.M116.725945. Epub 2016 May 2.

Structure of the GTP Form of Elongation Factor 4 (EF4) Bound to the Ribosome.

Author information

1
From the Institute of Molecular and Cell Biology, The Agency for Science, Technology and Research (A*STAR), 61 Biopolis Drive, 138673 Singapore, the School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, 637551 Singapore, and.
2
the School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, 637551 Singapore, and.
3
the School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, 637551 Singapore, and the Institute of Structural Biology, Nanyang Technological University, 636921 Singapore.
4
From the Institute of Molecular and Cell Biology, The Agency for Science, Technology and Research (A*STAR), 61 Biopolis Drive, 138673 Singapore, the School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, 637551 Singapore, and the Institute of Structural Biology, Nanyang Technological University, 636921 Singapore ygao@ntu.edu.sg.

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 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.

KEYWORDS:

EF4; LepA; cryo-EM; ribosome structure; translation; translation elongation factor; translational GTPase factor; translocation

PMID:
27137929
PMCID:
PMC4933213
DOI:
10.1074/jbc.M116.725945
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for HighWire Icon for PubMed Central
Loading ...
Support Center