Results 11 to 20 of about 7,251 (175)
Colicin E1 opens its hinge to plug TolC [PDF]
The double membrane architecture of Gram-negative bacteria forms a barrier that is impermeable to most extracellular threats. Bacteriocin proteins evolved to exploit the accessible, surface-exposed proteins embedded in the outer membrane to deliver ...
S Jimmy Budiardjo +9 more
doaj +4 more sources
Summary: The Escherichia coli outer membrane channel TolC complexes with several inner membrane efflux pumps to export compounds across the cell envelope. All components of these complexes are essential for robust efflux activity, yet E.
Shawna Zhu +10 more
doaj +3 more sources
An allosteric transport mechanism for the AcrAB-TolC multidrug efflux pump [PDF]
Bacterial efflux pumps confer multidrug resistance by transporting diverse antibiotics from the cell. In Gram-negative bacteria, some of these pumps form multi-protein assemblies that span the cell envelope.
Zhao Wang +8 more
doaj +5 more sources
Toxin import through the antibiotic efflux channel TolC [PDF]
AbstractBacteria often secrete diffusible protein toxins (bacteriocins) to kill bystander cells during interbacterial competition. Here, we use biochemical, biophysical and structural analyses to show how a bacteriocin exploits TolC, a major outer-membrane antibiotic efflux channel in Gram-negative bacteria, to transport itself across the outer ...
Housden, NG +7 more
openaire +4 more sources
Antibiotic-Sensitive TolC Mutants and Their Suppressors [PDF]
ABSTRACT The TolC protein of Escherichia coli , through its interaction with AcrA and AcrB, is thought to form a continuous protein channel that expels inhibitors from the cell. Consequently, tolC null mutations display a hypersensitive phenotype.
Anne Marie, Augustus +4 more
openaire +2 more sources
On the role of
SummaryTolC channel provides a route for the expelled drugs and toxins to cross the outer membrane of Escherichia coli. The puzzling feature of TolC structure is that the periplasmic entrance of the channel is closed by dense packing of 12 α‐helices. Efflux pumps exemplified by AcrAB are proposed to drive the opening of TolC channel.
Ganesh, Krishnamoorthy +3 more
openaire +2 more sources
Structure of the AcrAB–TolC multidrug efflux pump [PDF]
The capacity of numerous bacterial species to tolerate antibiotics and other toxic compounds arises in part from the activity of energy-dependent transporters. In Gram-negative bacteria, many of these transporters form multicomponent 'pumps' that span both inner and outer membranes and are driven energetically by a primary or secondary transporter ...
Du, Dijun +8 more
openaire +2 more sources
The Colicin E1 TolC-Binding Conformer: Pillar or Pore Function of TolC in Colicin Import? [PDF]
The mechanism by which the drug export protein TolC is utilized for import of the cytotoxin colicin E1 across the outer membrane and periplasmic space is addressed. Studies of the initial binding of colicin E1 with TolC, occlusion of membrane-incorporated TolC ion channels, and the structure underlying the colicin-TolC complex were based on the ...
Stanislav D, Zakharov +2 more
openaire +2 more sources
AcrA suppressor alterations reverse the drug hypersensitivity phenotype of a TolC mutant by inducing TolC aperture opening [PDF]
In Escherichia coli, the TolC-AcrAB complex forms a major antibiotic efflux system with broad substrate specificity. During the complex assembly, the periplasmic helices and bottom turns of TolC are thought to interact with a hairpin helix of AcrA and hairpin loops of AcrB respectively.
Jon W, Weeks +3 more
openaire +2 more sources
Role of TolC in Klebsiella oxytoca resistance to antibiotics [PDF]
The Gram-negative human pathogen Klebsiella oxytoca is often resistant to several antibiotics such as fluoroquinolones, erythromycin, tetracycline, chloramphenicol and others. The aim of this study was to look at the mechanisms leading to this resistance and particularly the role of TolC and efflux mechanisms in determining resistance.Ciprofloxacin ...
Anna, Fenosa +7 more
openaire +2 more sources

