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Structure and mode of action of clostridial glucosylating toxins: the ABCD model.
Rho-glucosylating Clostridium difficile toxins A and B: new insights into structure and function.
These studies, which provide new insights into structure, uptake, and function of the family of clostridial glucosylating toxins, are reviewed.
Clostridium difficile Toxin Biology.
C. difficile transferase toxin (CDT) is a binary actin-ADP-ribosylating toxin that causes depolymerization of actin, thereby inducing formation of the microtubule-based protrusions.
Auto-catalytic Cleavage of Clostridium difficile Toxins A and B Depends on Cysteine Protease Activity*
- Martina Egerer, T. Giesemann, T. Jank, Karla J. F. Satchell, K. Aktories
- Biology, ChemistryJournal of Biological Chemistry
- 31 August 2007
N-Ethylmaleimide blocked auto-cleavage induced by the addition of myo-inositol hexakisphosphate, suggesting that cysteine residues are essential for the processing of clostridial glucosylating toxins.
Clostridium difficile Glucosyltransferase Toxin B-essential Amino Acids for Substrate Binding*
Data from the solved crystal structure of the catalytic domain of Clostridium difficile toxin B allow the design of a model of the interaction of the glucosyltransferase domain of toxin B with its protein substrate RhoA, indicating that helix α17 is involved in RHoA recognition by toxin B.
Eddy Dissipation Rates in Thunderstorms Estimated by Doppler Radar in Relation to Aircraft In Situ Measurements
Abstract High-resolution aircraft turbulence measurements, well coordinated with radar Doppler spectral width measurements, have been used to verify radar-estimated energy dissipation rates within…
Structural basis for the function of Clostridium difficile toxin B.
Molecular Characteristics of Clostridium perfringens TpeL Toxin and Consequences of Mono-O-GlcNAcylation of Ras in Living Cells*
TpeL is a glucosylating toxin, which modifies Ras and induces apoptosis in target cells without having a typical C-terminal polypeptide repeat domain, and preferably utilizes UDP-N-acetylglucosamine (UDP-GlcNAc) as a sugar donor.
Bacillus sphaericus mosquitocidal toxin (MTX) and pierisin: the enigmatic offspring from the family of ADP‐ribosyltransferases
The recently solved crystal structure of MTX catalytic domain is helpful to reveal new insights into structural organization, catalytic mechanisms, proteolytic activation and autoinhibition of both enzymes.
Domain organization of Legionella effector SetA
- T. Jank, Kira E. Böhmer, Tina Tzivelekidis, Carsten Schwan, Y. Belyi, K. Aktories
- BiologyCellular Microbiology
- 1 June 2012
The data indicate that SetA is a multidomain protein with an N‐terminal glucosyltransferase domain and a C-terminal phosphatidylinositol 3‐phosphate‐binding domain, which guides the Legionella effector to the surface of the legionella‐containing vacuole.