Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/81200
Title: Structure of BipA in GTP form bound to the ratcheted ribosome
Authors: Kumar, Veerendra
Chen, Yun
Ero, Rya
Ahmed, Tofayel
Tan, Jackie
Li, Zhe
Wong, Andrew See Weng
Bhushan, Shashi
Gao, Yong-Gui
Keywords: Translational GTPase factors
X-ray crystallography
Cryo-electron microscopy
BipA
Ribosome
Issue Date: 2015
Source: Kumar, V., Chen, Y., Ero, R., Ahmed, T., Tan, J., Li, Z., et al. (2015). Structure of BipA in GTP form bound to the ratcheted ribosome. Proceedings of the National Academy of Sciences of the United States of America, 112(35), 10944-10949.
Series/Report no.: Proceedings of the National Academy of Sciences of the United States of America
Abstract: BPI-inducible protein A (BipA) is a member of the family of ribosome-dependent translational GTPase (trGTPase) factors along with elongation factors G and 4 (EF-G and EF4). Despite being highly conserved in bacteria and playing a critical role in coordinating cellular responses to environmental changes, its structures (isolated and ribosome bound) remain elusive. Here, we present the crystal structures of apo form and GTP analog, GDP, and guanosine-3′,5′-bisdiphosphate (ppGpp)-bound BipA. In addition to having a distinctive domain arrangement, the C-terminal domain of BipA has a unique fold. Furthermore, we report the cryo-electron microscopy structure of BipA bound to the ribosome in its active GTP form and elucidate the unique structural attributes of BipA interactions with the ribosome and A-site tRNA in the light of its possible function in regulating translation.
URI: https://hdl.handle.net/10356/81200
http://hdl.handle.net/10220/39160
DOI: 10.1073/pnas.1513216112
Rights: © 2015 The Author(s) (Published by National Academy of Sciences).This is the author created version of a work that has been peer reviewed and accepted for publication by Proceedings of the National Academy of Sciences of the United States of America, The Author(s) (Published by National Academy of Sciences). 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/10.1073/pnas.1513216112].
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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