Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/85549
Title: Similarity and diversity of translational GTPase factors EF-G, EF4, and BipA: From structure to function
Authors: Ero, Rya
Kumar, Veerendra
Chen, Yun
Gao, Yong-Gui
Keywords: BipA
EF-G
Issue Date: 2016
Source: Ero, R., Kumar, V., Chen, Y., & Gao, Y.-G. (2016). Similarity and diversity of translational GTPase factors EF-G, EF4, and BipA: From structure to function. RNA Biology, 13(12), 1258-1273.
Series/Report no.: RNA Biology
Abstract: EF-G, EF4, and BipA are members of the translation factor family of GTPases with a common ribosome binding mode and GTPase activation mechanism. However, topological variations of shared as well as unique domains ensure different roles played by these proteins during translation. Recent X-ray crystallography and cryo-electron microscopy studies have revealed the structural basis for the involvement of EF-G domain IV in securing the movement of tRNAs and mRNA during translocation as well as revealing how the unique C-terminal domains of EF4 and BipA interact with the ribosome and tRNAs contributing to the regulation of translation under certain conditions. EF-G, EF-4, and BipA are intriguing examples of structural variations on a common theme that results in diverse behavior and function. Structural studies of translational GTPase factors have been greatly facilitated by the use of antibiotics, which have revealed their mechanism of action.
URI: https://hdl.handle.net/10356/85549
http://hdl.handle.net/10220/43733
ISSN: 1547-6286
DOI: 10.1080/15476286.2016.1201627
Rights: © 2016 The Author(s). This is an Open Access article distributed under the terms of the Creative Commons Attribution-Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted.
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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