Structural and functional analogy between pneumolysin and proaerolysin |
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Authors: | Sowdhamini R; Mitchell TJ; Andrew PW; Morgan PJ |
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Affiliation: | Imperial Cancer Research Fund, Unit of Structural Molecular Biology, Department of Crystallography, Birkbeck College, UK. |
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Abstract: | 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.
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