ArticleProceedings of the National Academy of Sciences of the United States of America2015
Structure of BipA in GTP form bound to the ratcheted ribosome.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
- Article
- Direct genome-scale screening of Gluconobacter oxydans B58 for rare earth element bioleaching.Communications biology · 2025Article
- Role of the sarcin-ricin loop of 23S rRNA in biogenesis of the 50S ribosomal subunit.RNA (New York, N.Y.) · 2025Article
- Deep phosphoproteomics of Klebsiella pneumoniae reveals HipA-mediated tolerance to ciprofloxacin.PLoS pathogens · 2024Article
- New perspectives on the molecular mechanisms of stress signalling by the nucleotide guanosine tetraphosphate (ppGpp), an emerging regulator of photosynthesis in plants and algae.The New phytologist · 2023Review
- Novel rRNA transcriptional activity of NhaR revealed by its growth recovery for theFrontiers in molecular biosciences · 2023Article
- Article
- The Yersinia pestis GTPase BipA Promotes Pathogenesis of Primary Pneumonic Plague.Infection and immunity · 2021Article
- Functions and Regulation of Translation Elongation Factors.Frontiers in molecular biosciences · 2021Review
- Translational GTPase BipA Is Involved in the Maturation of a Large Subunit of Bacterial Ribosome at Suboptimal Temperature.Frontiers in microbiology · 2021Article
- A Global Ramachandran Score Identifies Protein Structures with Unlikely Stereochemistry.Structure (London, England : 1993) · 2020Article
- Functional Analysis of BipA in E. coli Reveals the Natural Plasticity of 50S Subunit Assembly.Journal of molecular biology · 2020Article
- The alarmones (p)ppGpp directly regulate translation initiation during entry into quiescence.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Elongation Factor Tu Switch I Element is a Gate for Aminoacyl-tRNA Selection.Journal of molecular biology · 2020Article
- Structural Analysis of (p)ppGpp Reveals Its Versatile Binding Pattern for Diverse Types of Target Proteins.Frontiers in microbiology · 2020Article
- Elucidation of a Novel Role of YebC in Surface Polysaccharides Regulation ofFrontiers in microbiology · 2020Article
- The Impact of the Stringent Response on TRAFAC GTPases and Prokaryotic Ribosome Assembly.Cells · 2019Review
- ABCF ATPases Involved in Protein Synthesis, Ribosome Assembly and Antibiotic Resistance: Structural and Functional Diversification across the Tree of Life.Journal of molecular biology · 2019Article
- New Insights into Ribosome Structure and Function.Cold Spring Harbor perspectives in biology · 2019Review
- The GTPase BipA expressed at low temperature inThe Journal of biological chemistry · 2018Article
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9 authors.
Funding
No grant is acknowledged in the PubMed record.
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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