Structural and functional characterisation of two proteolytic fragments of the bacterial protein toxin, pneumolysin

FEBS Letters

Rowe, Arthur J³  Harrison, Gayle²  Andrew, Peter W²  Freestone, Primrose P.E²  Morgan, Peter J²  Mitchell, Timothy J²  Gilbert, Robert J.C³  Crane, Dennis¹ 

[1] Laboratory of Molecular Structure, NIBSC, Blanche Lane, South Mimms, Potters Bar, Herts. EN6 3QG, UK;Department of Microbiology and Immunology, University of Leicester, Leicester, LE1 9HN, UK;NCMH, Department of Biochemistry, University of Leicester, Leicester, LE1 7RH, UK

关键词: Pneumolysin;    Domain structure and function;    Analytical ultracentrifugation;    Electron microscopy;    Circular dichroism;   

DOI  :  10.1016/S0014-5793(97)00838-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown