Faculty Opinions recommendation of A phenylalanine clamp catalyzes protein translocation through the anthrax toxin pore.

2005 ◽  
Author(s):  
Giampietro Schiavo
Keyword(s):  
Protein Translocation ◽  
Anthrax Toxin

scholarly journals Chemical Dissection of Protein Translocation through the Anthrax Toxin Pore

2011 ◽  
Vol 50 (10) ◽  
pp. 2294-2296 ◽  
Author(s):  
Brad L. Pentelute ◽  
Onkar Sharma ◽  
R. John Collier
Keyword(s):  
Protein Translocation ◽  
Anthrax Toxin

scholarly journals Ratcheting up protein translocation with anthrax toxin

2012 ◽  
Vol 21 (5) ◽  
pp. 606-624 ◽  
Author(s):  
Geoffrey K. Feld ◽  
Michael J. Brown ◽  
Bryan A. Krantz
Keyword(s):  
Protein Translocation ◽  
Anthrax Toxin

scholarly journals Ion selectivity of the anthrax toxin channel and its effect on protein translocation

2015 ◽  
Vol 146 (2) ◽  
pp. 183-192 ◽  
Author(s):  
Aviva Schiffmiller ◽  
Damon Anderson ◽  
Alan Finkelstein
Keyword(s):  
Protective Antigen ◽  
Protein Translocation ◽  
Ion Selectivity ◽  
Lethal Factor ◽  
Phospholipid Bilayer ◽  
Anthrax Toxin ◽  
Terminal Portion ◽  
Bilayer Membranes ◽  
Cation Selectivity ◽  
Edema Factor

Anthrax toxin consists of three ∼85-kD proteins: lethal factor (LF), edema factor (EF), and protective antigen (PA). PA63 (the 63-kD, C-terminal portion of PA) forms heptameric channels ((PA63)7) in planar phospholipid bilayer membranes that enable the translocation of LF and EF across the membrane. These mushroom-shaped channels consist of a globular cap domain and a 14-stranded β-barrel stem domain, with six anionic residues lining the interior of the stem to form rings of negative charges. (PA63)7 channels are highly cation selective, and, here, we investigate the effects on both cation selectivity and protein translocation of mutating each of these anionic residues to a serine. We find that although some of these mutations reduce cation selectivity, selectivity alone does not directly predict the rate of protein translocation; local changes in electrostatic forces must be considered as well.

Protein Translocation through the Anthrax Toxin Transmembrane Pore is Driven by a Proton Gradient

2006 ◽  
Vol 355 (5) ◽  
pp. 968-979 ◽  
Author(s):  
Bryan A. Krantz ◽  
Alan Finkelstein ◽  
R. John Collier
Keyword(s):  
Protein Translocation ◽  
Proton Gradient ◽  
Anthrax Toxin

scholarly journals Protein Translocation through Anthrax Toxin Channels Formed in Planar Lipid Bilayers

2004 ◽  
Vol 87 (6) ◽  
pp. 3842-3849 ◽  
Author(s):  
Sen Zhang ◽  
Eshwar Udho ◽  
Zhengyan Wu ◽  
R. John Collier ◽  
Alan Finkelstein
Keyword(s):  
Lipid Bilayers ◽  
Protein Translocation ◽  
Anthrax Toxin ◽  
Planar Lipid Bilayers

Tc Toxin Complexes: Assembly, Membrane Permeation, and Protein Translocation

2019 ◽  
Vol 73 (1) ◽  
pp. 247-265 ◽  
Author(s):  
Daniel Roderer ◽  
Stefan Raunser
Keyword(s):  
High Resolution ◽  
Functional Data ◽  
Protein Translocation ◽  
Conformational Transitions ◽  
Anthrax Toxin ◽  
Bacterial Toxin ◽  
Membrane Permeation ◽  
Human Pathogens ◽  
Host Membrane ◽  
And Function

Tc toxin complexes are virulence factors of many bacteria, including insect and human pathogens. Tc toxins are composed of three subunits that act together to perforate the host membrane, similar to a syringe, and translocate toxic enzymes into the host cell. The reactions of the toxic enzymes lead to deterioration and ultimately death of the cell. We review recent high-resolution structural and functional data that explain the mechanism of action of this type of bacterial toxin at an unprecedented level of molecular detail. We focus on the steps that are necessary for toxin activation and membrane permeation. This is where the largest conformational transitions appear. Furthermore, we compare the architecture and function of Tc toxins with those of anthrax toxin and vertebrate teneurin.

Sign in / Sign up

Export Citation Format

Share Document