Membrane-dependent conformational changes initiate cholesterol-dependent cytolysin oligomerization and intersubunit β-strand alignment

Author:

Ramachandran Rajesh,Tweten Rodney K,Johnson Arthur E

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Structural Biology

Reference20 articles.

1. Alouf, J.E. Introduction to the family of the structurally related cholesterol-binding cytolysins ('sulfhydryl-activated' toxins). In The Comprehensive Sourcebook of Bacterial Protein Toxins (eds. Alouf, J.E. & Freer, J.H.) 443–456 (Academic, London, 1999).

2. Tweten, R.K., Parker, M.W. & Johnson, A.E. The cholesterol-dependent cytolysins. Curr. Top. Microbiol. Immunol. 257, 15–33 (2001).

3. Olofsson, A., Hebert, H. & Thelestam, M. The projection structure of perfringolysin O (Clostridium perfringens Θ-toxin). FEBS Lett. 319, 125–127 (1993).

4. Rossjohn, J., Feil, S.C., Mckinstry, W.J., Tweten, R.K. & Parker, M.W. Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form. Cell 89, 685–692 (1997).

5. Heuck, A.P., Tweten, R.K. & Johnson, A.E. β-barrel pore forming toxins: intriguing dimorphic proteins. Biochemistry 40, 9065–9073 (2001).

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