Structural and functional analogy between pneumolysin and proaerolysin

Sowdhamini, R. ; Mitchell, T. J. ; Andrew, P. W. ; Morgan, P. J. (1997) Structural and functional analogy between pneumolysin and proaerolysin Protein Engineering Design and Selection, 10 (3). pp. 207-215. ISSN 1741-0126

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Pneumolysin and proaerolysin are bacterial toxins that form pores in host cells by oligomerization. We propose that they may have similar structures despite a poor sequence identity. The crystal structure of proaerolysin reveals a protein composed of four domains, arranged in the shape of an elongated comma. Electron microscopy of the pneumolysin monomer shows a similar arrangement of domains. The sequence of pneumolysin recognizes the template of proaerolysin from a library of protein folds. A three-dimensional model of pneumolysin has been constructed by the comparative approach using the structure of proaerolysin. This model, together with results on the activity of site-specific mutants and the positions of antigenic sites, has been used to propose functional roles of individual domains.

Item Type:Article
Source:Copyright of this article belongs to Oxford University Press.
Keywords:Distant Relationship; Pore-forming Toxins; Structure Prediction and Three-dimensional Modelling; Superfamily; Thiol-activated Cytolysins
ID Code:61268
Deposited On:15 Sep 2011 03:53
Last Modified:15 Sep 2011 03:53

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