Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/81842
Title: Structure of the GTP Form of Elongation Factor 4 (EF4) Bound to the Ribosome
Authors: Kumar, Veerendra
Ero, Rya
Ahmed, Tofayel
Goh, Kwok Jian
Zhan, Yin
Bhushan, Shashi
Gao, Yong-Gui
Keywords: Cryo-EM
Ribosome structure
Issue Date: 2016
Source: Kumar, V., Ero, R., Ahmed, T., Goh, K. J., Zhan, Y., Bhushan, S., et al. (2016). Structure of the GTP Form of Elongation Factor 4 (EF4) Bound to the Ribosome. The Journal of Biological Chemistry, 291(25), 12943-12950.
Series/Report no.: The Journal of Biological Chemistry
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.
URI: https://hdl.handle.net/10356/81842
http://hdl.handle.net/10220/43494
ISSN: 0021-9258
DOI: 10.1074/jbc.M116.725945
Rights: © 2016 The American Society for Biochemistry and Molecular Biology (ASBMB). This is the author created version of a work that has been peer reviewed and accepted for publication by The Journal of Biological Chemistry, The American Society for Biochemistry and Molecular Biology. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: [http://dx.doi.org/10.1074/jbc.M116.725945].
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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