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

Content Provider	Scilit
Author	Kumar, Veerendra Ero, Rya Ahmed, Tofayel Goh, Kwok Jian Zhan, Yin Bhushan, Shashi Gao, Yong-Gui
Copyright Year	2016
Description	Journal: Journal of Biological Chemistry 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.
Related Links	http://www.jbc.org/content/291/25/12943.full.pdf https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4933213/pdf http://www.jbc.org/article/S0021925820394412/pdf
Ending Page	12950
Page Count	8
Starting Page	12943
ISSN	00219258
e-ISSN	1083351X
DOI	10.1074/jbc.m116.725945
Journal	Journal of Biological Chemistry
Issue Number	25
Volume Number	291
Language	English
Publisher	Elsevier BV
Publisher Date	2016-06-01
Access Restriction	Open
Subject Keyword	Journal: Journal of Biological Chemistry Ribosome Structure Translation Elongation Factor Translational Gtpase Factor
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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