ArticleBiophysical journal2008
Gating at both ends and breathing in the middle: conformational dynamics of TolC.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
19 citing papers in PubMed, 61 citations in OpenAlex.
- The Resistance-Nodulation-Division efflux pump EefABC is highly conserved within lineages ofMicrobial genomics · 2026Article
- Structural shifts in TolC facilitate Efflux-Mediated β-lactam resistance.Communications biology · 2024Article
- Conformational dynamics and putative substrate extrusion pathways of the N-glycosylated outer membrane factor CmeC from Campylobacter jejuni.PLoS computational biology · 2023Article
- What have molecular simulations contributed to understanding of Gram-negative bacterial cell envelopes?Microbiology (Reading, England) · 2022Review
- Common recognition topology of mex transporters ofFrontiers in pharmacology · 2022Article
- Lpp positions peptidoglycan at the AcrA-TolC interface in the AcrAB-TolC multidrug efflux pump.Biophysical journal · 2021Article
- Structure, Assembly, and Function of Tripartite Efflux and Type 1 Secretion Systems in Gram-Negative Bacteria.Chemical reviews · 2021Review
- Conformational Dynamics of AcrA Govern Multidrug Efflux Pump Assembly.ACS infectious diseases · 2019Article
- Efflux Pumps Represent Possible Evolutionary Convergence onto the β-Barrel Fold.Structure (London, England : 1993) · 2018Article
- Crystal structure of an antigenic outer-membrane protein from Salmonella Typhi suggests a potential antigenic loop and an efflux mechanism.Scientific reports · 2015Article
- Focus on the Outer Membrane Factor OprM, the Forgotten Player from Efflux Pumps Assemblies.Antibiotics (Basel, Switzerland) · 2015Review
- Interaction of antibacterial compounds with RND efflux pumps in Pseudomonas aeruginosa.Frontiers in microbiology · 2015Review
- Assembly and stability of Salmonella enterica ser. Typhi TolC protein in POPE and DMPE.Journal of biological physics · 2014Article
- Structural mechanisms of heavy-metal extrusion by the Cus efflux system.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2013Article
- Molecular Dynamics Computer Simulations of Multidrug RND Efflux Pumps.Computational and structural biotechnology journal · 2013Review
- Structure and mechanism of the tripartite CusCBA heavy-metal efflux complex.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Review
- Functional rotation of the transporter AcrB: insights into drug extrusion from simulations.PLoS computational biology · 2010Article
- Trinity revealed: Stoichiometric complex assembly of a bacterial multidrug efflux pump.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Transitions between closed and open conformations of TolC: the effects of ions in simulations.Biophysical journal · 2009Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Drug extrusion via efflux through a tripartite complex (an inner membrane pump, an outer membrane protein, and a periplasmic protein) is a widely used mechanism in Gram-negative bacteria. The outer membrane protein (TolC in Escherichia coli; OprM in Pseudomonas aeruginosa) forms a tunnel-like pore through the periplasmic space and the outer membrane. Molecular dynamics simulations of TolC have been performed, and are compared to simulations of Y362F/R367S mutant, and to simulations of its homolog OprM. The results reveal a complex pattern of conformation dynamics in the TolC protein. Two putative gate regions, located at either end of the protein, can be distinguished. These regions are the extracellular loops and the mouth of the periplasmic domain, respectively. The periplasmic gate has been implicated in the conformational changes leading from the closed x-ray structure to a proposed open state of TolC. Between the two gates, a peristaltic motion of the periplasmic domain is observed, which may facilitate transport of the solutes from one end of the tunnel to the other. The motions observed in the atomistic simulations are also seen in coarse-grained simulations in which the protein tertiary structure is represented by an elastic network model.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.