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Journal ArticleDOI

A “Drug Sweeping” State of the TriABC Triclosan Efflux Pump from Pseudomonas aeruginosa

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TLDR
It is proposed that selective substrate translocation involves conformational gating at the tunnel narrowing that, together with conformational ordering of TriA and TriB, creates an engaged state capable of mediating substrate efflux.
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This article is published in Structure.The article was published on 2021-03-04. It has received 7 citations till now. The article focuses on the topics: Membrane fusion protein & Periplasmic space.

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Structure, Assembly, and Function of Tripartite Efflux and Type 1 Secretion Systems in Gram-Negative Bacteria

TL;DR: In this article, the authors summarize the recent advances in understanding of structural biology, function, and regulation of these systems, highlighting the previously undescribed role of periplasmic adaptor proteins (PAPs) in providing a common architectural scaffold across diverse families of transporters.
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Disinfectant resistance in bacteria: Mechanisms, spread, and resolution strategies.

TL;DR: In this article, a review focused on the resistance mechanisms of disinfectant resistant bacteria on biofilms, cell membrane permeability, efflux pumps, degradable enzymes, and disinfectant targets.
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Ever-Adapting RND Efflux Pumps in Gram-Negative Multidrug-Resistant Pathogens: A Race against Time.

TL;DR: In this article, the authors take a closer look at clinically, environmentally and laboratory-evolved Gram-negative bacterial strains and their decreased drug sensitivity as a result of mutations directly in the RND-type pumps themselves (from Escherichia coli, Salmonella-enterica, Neisseria gonorrhoeae, Pseudomonas aeruginosa, Acinetobacter baumannii and Legionella pneumophila).
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The Whole Is Bigger than the Sum of Its Parts: Drug Transport in the Context of Two Membranes with Active Efflux.

TL;DR: In this paper, the authors present a review of key experimental and computational approaches to the investigation of transport by individual translocators and in whole cells, summarizes key findings from these studies and outlines implications for antibiotic discovery.
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Multidrug Efflux Pumps and the Two-Faced Janus of Substrates and Inhibitors.

TL;DR: In this article, the authors discuss intriguing relationships between substrates and inhibitors of efflux pumps, as these two types of ligands face similar barriers and binding sites in the transporters and accessory proteins and both types of activities often occur with the same chemical scaffold.
References
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Journal ArticleDOI

MOLEonline: a web-based tool for analyzing channels, tunnels and pores (2018 update).

TL;DR: The updated version of MOLEonline overcomes limitations of the previous version by incorporating the recently developed LiteMol Viewer visualization engine and providing a simple, fully interactive user experience.
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An allosteric transport mechanism for the AcrAB-TolC Multidrug Efflux Pump.

TL;DR: The near-atomic resolution cryoEM structures of the Escherichia coli AcrAB-TolC multidrug efflux pump in resting and drug transport states are reported, revealing a quaternary structural switch that allosterically couples and synchronizes initial ligand binding with channel opening.
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MonoRes: Automatic and Accurate Estimation of Local Resolution for Electron Microscopy Maps

TL;DR: A fully automatic, accurate method for determining the local resolution of a 3D map (MonoRes), which is computationally more rapid than existing methods in the field and offers the option of local filtering of the original map based on the calculated local resolution.
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Chimeric Analysis of the Multicomponent Multidrug Efflux Transporters from Gram-Negative Bacteria

TL;DR: The results suggest that the large periplasmic loops of RND-type transporters are involved in multidrug recognition and efflux.
Journal ArticleDOI

Arginine residues at internal positions in a protein are always charged

TL;DR: It is shown that, in contrast to a systematic study of Lys, Asp, and Glu residues at 25 internal positions in staphylococcal nuclease, Arg residues at the same internal positions exhibit no detectable shifts in pKa; they are all charged at pH ≤ 10.
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