ArticleThe Journal of biological chemistry2015
Structure and function of the Escherichia coli Tol-Pal stator protein TolR.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 54 citations in OpenAlex.
- Bacteriocin biophysics: From protein-protein interaction models to navigators of the bacterial cell envelope.The Journal of biological chemistry · 2026Article
- Advances in understanding Ton and Tol system motor proteins.Biochemical Society transactions · 2026Review
- Deciphering the molecular mechanism of the bacterial division motor TolQRA.Cell discovery · 2025Article
- An inner membrane protein is covalently attached to peptidoglycan in the γ-proteobacterium Dickeya dadantii.Communications biology · 2025Article
- Cryo-EM structures of the E. coli Ton and Tol motor complexes.Nature communications · 2025Article
- Hypervesiculation Meets Sec-Targeting: Enhancing Heterologous Protein Loading inInternational journal of molecular sciences · 2025Article
- Structural architecture of TolQ-TolR inner membrane protein complex from opportunistic pathogenScience advances · 2025Article
- Article
- The Tol Pal system integrates maintenance of the three layered cell envelope.npj antimicrobials and resistance · 2024Review
- Ton motor conformational switch and peptidoglycan role in bacterial nutrient uptake.Nature communications · 2024Article
- Development of aFrontiers in microbiology · 2024Article
- Cell division cycle fluctuation of Pal concentration in Escherichia coli.Access microbiology · 2024Article
- Exploring Flexibility and Folding Patterns Throughout Time in Voltage Sensors.Journal of molecular evolution · 2023Article
- Tunable force transduction through theProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Energization of Outer Membrane Transport by the ExbB ExbD Molecular Motor.Journal of bacteriology · 2023Review
- Chasing long-range evolutionary couplings in the AlphaFold era.Biopolymers · 2023Article
- Making a chink in their armor: Current and next-generation antimicrobial strategies against the bacterial cell envelope.Advances in microbial physiology · 2023Article
- What have molecular simulations contributed to understanding of Gram-negative bacterial cell envelopes?Microbiology (Reading, England) · 2022Review
- A new class of biological ion-driven rotary molecular motors with 5:2 symmetry.Frontiers in microbiology · 2022Review
- Force-Generation by the Trans-Envelope Tol-Pal System.Frontiers in microbiology · 2022Review
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
TolR is a 15-kDa inner membrane protein subunit of the Tol-Pal complex in Gram-negative bacteria, and its function is poorly understood. Tol-Pal is recruited to cell division sites where it is involved in maintaining the integrity of the outer membrane. TolR is related to MotB, the peptidoglycan (PG)-binding stator protein from the flagellum, suggesting it might serve a similar role in Tol-Pal. The only structure thus far reported for TolR is of the periplasmic domain from Haemophilus influenzae in which N- and C-terminal residues had been deleted (TolR(62-133), Escherichia coli numbering). H. influenzae TolR(62-133) is a symmetrical dimer with a large deep cleft at the dimer interface. Here, we present the 1.7-Å crystal structure of the intact periplasmic domain of E. coli TolR (TolR(36-142)). E. coli TolR(36-142) is also dimeric, but the architecture of the dimer is radically different from that of TolR(62-133) due to the intertwining of its N and C termini. TolR monomers are rotated ∼180° relative to each other as a result of this strand swapping, obliterating the putative PG-binding groove seen in TolR(62-133). We found that removal of the strand-swapped regions (TolR(60-133)) exposes cryptic PG binding activity that is absent in the full-length domain. We conclude that to function as a stator in the Tol-Pal complex dimeric TolR must undergo large scale structural remodeling reminiscent of that proposed for MotB, where the N- and C-terminal sequences unfold in order for the protein to both reach and bind the PG layer ∼90 Å away from the inner membrane.
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