ArticleStructure (London, England : 1993)2017
The BID Domain of Type IV Secretion Substrates Forms a Conserved Four-Helix Bundle Topped with a Hook.
Article in Structure (London, England : 1993), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 22 citations in OpenAlex.
- A subset of type 4 secretion system effectors ofmicroLife · 2026Article
- Anchorage of bacterial effector at plasma membrane via selective phosphatidic acid binding to modulate host cell signaling.PLoS pathogens · 2024Article
- Translocation of YopJ family effector proteins through the VirB/VirD4 T4SS ofProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Phytochrome-Interacting Proteins.Biomolecules · 2023Review
- Structural basis for effector recognition by an antibacterial type IV secretion system.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Evolutionary Diversification of Host-TargetedMicroorganisms · 2021Article
- Type IV secretion systems: Advances in structure, function, and activation.Molecular microbiology · 2021Review
- The Impact ofFrontiers in microbiology · 2021Review
- Bartonella effector protein C mediates actin stress fiber formation via recruitment of GEF-H1 to the plasma membrane.PLoS pathogens · 2021Article
- Role of distinct type-IV-secretion systems and secreted effector sets in host adaptation by pathogenic Bartonella species.Cellular microbiology · 2019Review
- Versatility of the BID Domain: Conserved Function as Type-IV-Secretion-Signal and Secondarily Evolved Effector Functions WithinFrontiers in microbiology · 2019Review
- A bacterial toxin-antitoxin module is the origin of inter-bacterial and inter-kingdom effectors of Bartonella.PLoS genetics · 2017Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
The BID (Bep intracellular delivery) domain functions as secretion signal in a subfamily of protein substrates of bacterial type IV secretion (T4S) systems. It mediates transfer of (1) relaxases and the attached DNA during bacterial conjugation, and (2) numerous Bartonella effector proteins (Beps) during protein transfer into host cells infected by pathogenic Bartonella species. Furthermore, BID domains of Beps have often evolved secondary effector functions within host cells. Here, we provide crystal structures for three representative BID domains and describe a novel conserved fold characterized by a compact, antiparallel four-helix bundle topped with a hook. The conserved hydrophobic core provides a rigid scaffold to a surface that, despite a few conserved exposed residues and similarities in charge distribution, displays significant variability. We propose that the genuine function of BID domains as T4S signal may primarily depend on their rigid structure, while the plasticity of their surface may facilitate adaptation to secondary effector functions.
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