Structure of BipA in GTP form bound to the ratcheted ribosome

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Structure of BipA in GTP form bound to the ratcheted ribosome
Title:
Structure of BipA in GTP form bound to the ratcheted ribosome
Journal Title:
Proceedings of the National Academy of Sciences
Keywords:
Publication Date:
17 August 2015
Citation:
Veerendra Kumar, Yun Chen, Rya Ero, Tofayel Ahmed, Jackie Tan, Zhe Li, Andrew See Weng Wong, Shashi Bhushan, and Yong-Gui Gao Structure of BipA in GTP form bound to the ratcheted ribosome PNAS 2015 112 (35) 10944-10949; published ahead of print August 17, 2015, doi:10.1073/pnas.1513216112
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.
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Full paper can be downloaded from the Publisher's URL provided.
ISSN:
1091-6490
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