ArticleProtein & cell2016
Structural insights into the regulatory mechanism of the Pseudomonas aeruginosa YfiBNR system.
Article in Protein & cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 25 citations in OpenAlex.
- Genetic diversification ofApplied and environmental microbiology · 2026Article
- Virulence regulation in the fish pathogenFrontiers in cellular and infection microbiology · 2026Review
- Mixed-species interactions constrain diversification and shape biofilm evolution.ISME communications · 2026Article
- Student-led experimental evolution reveals novel biofilm regulators of adaptation to multiple niches.bioRxiv : the preprint server for biology · 2025Article
- Dataset from a human-in-the-loop approach to identify functionally important protein residues from literature.Scientific data · 2024Article
- Spatial transcriptome uncovers rich coordination of metabolism in E. coli K12 biofilm.Nature chemical biology · 2023Article
- Nucleotide second messengers in bacterial decision making.Current opinion in microbiology · 2020Review
- Article
- Temperature-Dependent Gene Expression inFrontiers in microbiology · 2018Article
- Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
YfiBNR is a recently identified bis-(3'-5')-cyclic dimeric GMP (c-di-GMP) signaling system in opportunistic pathogens. It is a key regulator of biofilm formation, which is correlated with prolonged persistence of infection and antibiotic drug resistance. In response to cell stress, YfiB in the outer membrane can sequester the periplasmic protein YfiR, releasing its inhibition of YfiN on the inner membrane and thus provoking the diguanylate cyclase activity of YfiN to induce c-di-GMP production. However, the detailed regulatory mechanism remains elusive. Here, we report the crystal structures of YfiB alone and of an active mutant YfiB(L43P) complexed with YfiR with 2:2 stoichiometry. Structural analyses revealed that in contrast to the compact conformation of the dimeric YfiB alone, YfiB(L43P) adopts a stretched conformation allowing activated YfiB to penetrate the peptidoglycan (PG) layer and access YfiR. YfiB(L43P) shows a more compact PG-binding pocket and much higher PG binding affinity than wild-type YfiB, suggesting a tight correlation between PG binding and YfiB activation. In addition, our crystallographic analyses revealed that YfiR binds Vitamin B6 (VB6) or L-Trp at a YfiB-binding site and that both VB6 and L-Trp are able to reduce YfiB(L43P)-induced biofilm formation. Based on the structural and biochemical data, we propose an updated regulatory model of the YfiBNR system.
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