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Chaperone Dependent Assembly and Structure of a Bacterial Polypeptide Capsule

Institutions
University of Reading
Start date
2002
End date
2005
Objective
F1 capsule is a polymer of a single subunit assembled on the surface of Yersinia pestis by the chaperone/usher pathway. Having blocked polymerisation of subunit and produced for the first time stable binary chaperone:subunit complex, the three-dimensional structure of the complex will be solved by X-ray crystallography. Polymer structure will be investigated by mass spectrometry, atomic force microscopy and crystallisation of mutants producing stable ternary chaperone:subunit2 complex. Mutagenesis will complement structural studies and be used to create stable subunit monomer.

Results will provide detail on folding and polymerisation of relevance to all of this subfamily of adhesive organelles, including those of pathogenic E. coli and Salmonella spp.

Funding Source
Biotechnology and Biological Sciences Research Council
Project number
B16926
Categories
Salmonella
Escherichia coli