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Research article2003Peer reviewedOpen access

Structure and biogenesis of the capsular F1 antigen from Yersinia pestis: Preserved folding energy drives fiber formation

Zavialov AV, Berglund J, Pudney AF, Fooks LJ, Ibrahim TM, MacIntyre S, Knight SD

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

    • Zavialov, Anton

      • Department of Molecular Biology, Swedish University of Agricultural Sciences
      • Berglund, Jenny

        • Department of Molecular Biology, Swedish University of Agricultural Sciences
        • Knight, Stefan David

          • 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