Zavialov, Anton
- Department of Molecular Biology, Swedish University of Agricultural Sciences
Abstract
Most gram-negative pathogens express fibrous adhesive virulence organelles that mediate targeting to the sites of infection. The F1 capsular antigen from the plague pathogen Yersinia pestis consists of linear fibers of a single subunit (Caf1) and serves as a prototype for nonpilus organelles assembled via the chaperone/usher pathway. Genetic data together with high-resolution X-ray structures corresponding to snapshots of the assembly process reveal the structural basis of fiber formation. Comparison of chaperone bound Caf1 subunit with the subunit in the fiber reveals a novel type of conformational change involving the entire hydrophobic core of the protein. The observed conformational change suggests that the chaperone traps a high-energy folding intermediate of Caf1. A model is proposed in which release of the subunit allows folding to be completed, driving fiber formation
Published in
Cell
2003, volume: 113, number: 5, pages: 587-596
Publisher: CELL PRESS
SLU Authors
Berglund, Jenny
- Department of Molecular Biology, Swedish University of Agricultural Sciences
- Department of Molecular Biology, Swedish University of Agricultural Sciences
Knight, Stefan David
- Department of Molecular Biology, Swedish University of Agricultural Sciences
- Department of Molecular Biology, Swedish University of Agricultural Sciences
UKÄ Subject classification
Food Science
Publication identifier
- DOI: https://doi.org/10.1016/S0092-8674(03)00351-9
Permanent link to this page (URI)
https://res.slu.se/id/publ/141