ArticleThe EMBO journal2002
Structure of the periplasmic domain of Pseudomonas aeruginosa TolA: evidence for an evolutionary relationship with the TonB transporter protein.
Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- 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
- Origin and Evolution of Bacterial Periplasmic Force Transducers.Molecular biology and evolution · 2025Article
- Structural architecture of TolQ-TolR inner membrane protein complex from opportunistic pathogenScience advances · 2025Article
- Tunable force transduction through theProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Recruitment of the TolA Protein to Cell Constriction Sites in Escherichia coli via Three Separate Mechanisms, and a Critical Role for FtsWI Activity in Recruitment of both TolA and TolQ.Journal of bacteriology · 2022Article
- 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
- The quantitative basis for the redistribution of immobile bacterial lipoproteins to division septa.PLoS computational biology · 2021Article
- The multifarious roles of Tol-Pal in Gram-negative bacteria.FEMS microbiology reviews · 2020Review
- The lipoprotein Pal stabilises the bacterial outer membrane during constriction by a mobilisation-and-capture mechanism.Nature communications · 2020Article
- Structure and Stoichiometry of the Ton Molecular Motor.International journal of molecular sciences · 2020Review
- Article
- Structural evidence that colicin A protein binds to a novel binding site of TolA protein in Escherichia coli periplasm.The Journal of biological chemistry · 2012Article
- Legionella pneumophila LbtU acts as a novel, TonB-independent receptor for the legiobactin siderophore.Journal of bacteriology · 2011Article
- Swimming against the tide: progress and challenges in our understanding of colicin translocation.Nature reviews. Microbiology · 2010Review
- A Novel extracytoplasmic function (ECF) sigma factor regulates virulence in Pseudomonas aeruginosa.PLoS pathogens · 2009Article
- Energy-dependent immunity protein release during tol-dependent nuclease colicin translocation.The Journal of biological chemistry · 2009Article
- Colicin biology.Microbiology and molecular biology reviews : MMBR · 2007Review
- Biological role and structural mechanism of twinfilin-capping protein interaction.The EMBO journal · 2004Article
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7 authors.
Funding
Abstract
The crystal structure of the C-terminal domain III of Pseudomonas aeruginosa TolA has been determined at 1.9 A resolution. The fold is similar to that of the corresponding domain of Escherichia coli TolA, despite the limited amino acid sequence identity of the two proteins (20%). A pattern was discerned that conserves the fold of domain III within the wider TolA family and, moreover, reveals a relationship between TolA domain III and the C-terminal domain of the TonB transporter proteins. We propose that the TolA and TonB C-terminal domains have a common evolutionary origin and are related by means of domain swapping, with interesting mechanistic implications. We have also determined the overall shape of the didomain, domains II + III, of P.aeruginosa TolA by solution X-ray scattering. The molecule is monomeric-its elongated, stalk shape can accommodate the crystal structure of domain III at one end, and an elongated helical bundle within the portion corresponding to domain II. Based on these data, a model for the periplasmic domains of P.aeruginosa TolA is presented that may explain the inferred allosteric properties of members of the TolA family. The mechanisms of TolA-mediated entry of bateriophages in P.aeruginosa and E.coli are likely to be similar.
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