Journal article
Structures of perfringolysin O suggest a pathway for activation of cholesterol-dependent cytolysins
Jamie Rossjohn, Galina Polekhina, Susanne C Feil, Craig J Morton, Rodney K Tweten, Michael W Parker
JOURNAL OF MOLECULAR BIOLOGY | ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD | Published : 2007
Abstract
Cholesterol-dependent cytolysins (CDCs), a large family of bacterial toxins, are secreted as water-soluble monomers and yet are capable of generating oligomeric pores in membranes. Previous work has demonstrated that large scale structural rearrangements occur during this transition but the detailed mechanism by which these changes take place remains a puzzle. Despite evidence of structural and functional couplings between domains 3 and 4, the crystal structure of the CDC, perfringolysin O (PFO), shows the two domains do not make direct contact. Here, we present crystal structures of PFO that demonstrate movements of domain 4 are sufficient to trigger conformational changes that are transmit..
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Awarded by NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES
Awarded by NIAID NIH HHS