title: Toxin structure: part of a hole?
abstract: The structure of the monomeric form of perfringolysin O solved by X-ray crystallography has been used to model the very large transmembrane pore formed when this bacterial protein toxin assembles in cholesterol-containing membranes. The structure is a notable advance, but it may not provide the whole story.
authors.affiliation: Department of Medical Biochemistry and Genetics, Texas A&M Health Science Center, 440 Reynolds Medical Building, College Station, Texas 77843-1114, USA. bayley@tamu.edu
authors.forename: H
authors.initials: H
authors.lastname: Bayley
mesh_terms: D001427:Bacterial Toxins / Q000737:chemistry* / Q000378:metabolism; D002784:Cholesterol / Q000378:metabolism; D003016:Clostridium perfringens / Q000378:metabolism; D018360:Crystallography, X-Ray; D006460:Hemolysin Proteins; D008051:Lipid Bilayers / Q000378:metabolism; D008954:Models, Biological; D011487:Protein Conformation
chemical_list: D001427:Bacterial Toxins; D006460:Hemolysin Proteins; D008051:Lipid Bilayers; C020452:Clostridium perfringens theta-toxin; D002784:Cholesterol