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Mechanism of membrane insertion of a multimeric beta-barrel protein: perfringolysin O creates a pore using ordered and coupled conformational changes.

Abstract：

:Perfringolysin O, a bacterial cytolytic toxin, forms unusually large pores in cholesterol-containing membranes by the spontaneous insertion of two of its four domains into the bilayer. By monitoring the kinetics of domain-specific conformational changes and pore formation using fluorescence spectroscopy, the temporal sequence of domain-membrane interactions has been established. One membrane-exposed domain does not penetrate deeply into the bilayer and is not part of the actual pore, but is responsible for membrane recognition. This domain must bind to the membrane before insertion of the other domain into the bilayer is initiated. The two domains are conformationally coupled, even though they are spatially separated. Thus, cytolytic pore formation is accomplished by a novel mechanism of ordered conformational changes and interdomain communication.

journal_name

Mol Cell

journal_title

Molecular cell

authors

Heuck AP,Hotze EM,Tweten RK,Johnson AE

doi

10.1016/s1097-2765(00)00119-2

subject

Has Abstract

pub_date

2000-11-01 00:00:00

pages

1233-42

issue

5

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(00)00119-2

journal_volume

6

pub_type

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