title: Structural and functional characterisation of two proteolytic fragments of the bacterial protein toxin, pneumolysin.
abstract: Proteolytic cleavage of the bacterial protein toxin pneumolysin with protease K creates two fragments of 37 and 15 kDa. This paper describes the purification of these two fragments and their subsequent physical and biological characterisation. The larger fragment is directly involved in the cytolytic mechanism of this pore-forming protein, via membrane binding and self-association. The smaller fragment lacks ordered structure or discernible activity.
authors.affiliation: Department of Microbiology and Immunology, University of Leicester, UK.
authors.forename: P J
authors.initials: PJ
authors.lastname: Morgan
authors.forename: G
authors.initials: G
authors.lastname: Harrison
authors.forename: P P
authors.initials: PP
authors.lastname: Freestone
authors.forename: D
authors.initials: D
authors.lastname: Crane
authors.forename: A J
authors.initials: AJ
authors.lastname: Rowe
authors.forename: T J
authors.initials: TJ
authors.lastname: Mitchell
authors.forename: P W
authors.initials: PW
authors.lastname: Andrew
authors.forename: R J
authors.initials: RJ
authors.lastname: Gilbert
mesh_terms: D001426:Bacterial Proteins; D002942:Circular Dichroism; D019286:Endopeptidase K; D006461:Hemolysis; D006868:Hydrolysis; D008081:Liposomes / Q000378:metabolism; D010446:Peptide Fragments / Q000737:chemistry* / Q000302:isolation & purification / Q000502:physiology*; D011485:Protein Binding; D013050:Spectrometry, Fluorescence; D013301:Streptolysins / Q000737:chemistry* / Q000302:isolation & purification / Q000502:physiology*; D013329:Structure-Activity Relationship
chemical_list: D001426:Bacterial Proteins; D008081:Liposomes; D010446:Peptide Fragments; D013301:Streptolysins; C032290:plY protein, Streptococcus pneumoniae; D019286:Endopeptidase K