title: How cholesterol-dependent cytolysins bite holes into membranes.
abstract: In a show piece for electron microscopy (EM), Tilley at al. used single-particle cryo-EM to visualize the structural rearrangements in the bacterial toxin pneumolysin that occur when it assembles into a membrane-associated prepore and when the prepore subsequently transitions into a fully membrane-inserted pore.
authors.affiliation: Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, USA. twalz@hms.harvard.edu
authors.forename: Thomas
authors.initials: T
authors.lastname: Walz
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism* / Q000648:ultrastructure; D002784:Cholesterol / Q000378:metabolism*; D020285:Cryoelectron Microscopy; D003603:Cytotoxins / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D013301:Streptolysins / Q000737:chemistry / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D003603:Cytotoxins; D013301:Streptolysins; C032290:plY protein, Streptococcus pneumoniae; D002784:Cholesterol