ArticleScientific reports2015
Structural insights into YfiR sequestering by YfiB in Pseudomonas aeruginosa PAO1.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 19 citations in OpenAlex.
- Mixed-species interactions constrain diversification and shape biofilm evolution.ISME communications · 2026Article
- Diospyros kaki L. (persimmon) as a potential antibiofilm agent against Acinetobacter pittii, Acinetobacter baumannii, and Pseudomonas aeruginosa isolated from diabetic foot patients.World journal of microbiology & biotechnology · 2025Article
- Training bias and sequence alignments shape protein-peptide docking by AlphaFold and related methods.Protein science : a publication of the Protein Society · 2025Article
- YfiB: An Outer Membrane Protein Involved in the Virulence ofMicroorganisms · 2022Article
- Evolved resistance to a novel cationic peptide antibiotic requires high mutation supply.Evolution, medicine, and public health · 2022Article
- Promysalin Elicits Species-Selective Inhibition of Pseudomonas aeruginosa by Targeting Succinate Dehydrogenase.Journal of the American Chemical Society · 2018Article
- HmsC ControlsFrontiers in cellular and infection microbiology · 2017Article
- Biofilms and Cyclic di-GMP (c-di-GMP) Signaling: Lessons from Pseudomonas aeruginosa and Other Bacteria.The Journal of biological chemistry · 2016Review
- Structural insights into the regulatory mechanism of the Pseudomonas aeruginosa YfiBNR system.Protein & cell · 2016Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
YfiBNR is a tripartite signalling system in Pseudomonas aeruginosa that modulates intracellular c-di-GMP levels in response to signals received in the periplasm. YfiB is an outer membrane lipoprotein and presumed sensor protein that sequesters the repressor protein YfiR. To provide insights into YfiBNR function, we have determined three-dimensional crystal structures of YfiB and YfiR from P. aeruginosa PAO1 alone and as a 1:1 complex. A YfiB(27-168) construct is predominantly dimeric, whereas a YfiB(59-168) is monomeric, indicating that YfiB can dimerize via its N-terminal region. YfiR forms a stable complex with YfiB(59-168), while the YfiR binding interface is obstructed by the N-terminal region in YfiB(27-168). The YfiB-YfiR complex reveals a conserved interaction surface on YfiR that overlaps with residues predicted to interact with the periplasmic PAS domain of YfiN. Comparison of native and YfiR-bound structures of YfiB suggests unwinding of the N-terminal linker region for attachment to the outer membrane. A model is thus proposed for YfiR sequestration at the outer membrane by YfiB. Our work provides the first detailed insights into the interaction between YfiB and YfiR at the molecular level and is a valuable starting point for further functional and mechanistic studies of the YfiBNR signalling system.
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