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Science 13 August 1999:
Vol. 285. no. 5430, pp. 1058 - 1061
DOI: 10.1126/science.285.5430.1058

Reports

Structural Basis of Chaperone Function and Pilus Biogenesis

Frederic G. Sauer, 1* Klaus Fütterer, 2* Jerome S. Pinkner, 1 Karen W. Dodson, 1 Scott J. Hultgren, 1dagger Gabriel Waksman 2dagger

Many Gram-negative pathogens assemble architecturally and functionally diverse adhesive pili on their surfaces by the chaperone-usher pathway. Immunoglobulin-like periplasmic chaperones escort pilus subunits to the usher, a large protein complex that facilitates the translocation and assembly of subunits across the outer membrane. The crystal structure of the PapD-PapK chaperone-subunit complex, determined at 2.4 angstrom resolution, reveals that the chaperone functions by donating its G1 beta  strand to complete the immunoglobulin-like fold of the subunit via a mechanism termed donor strand complementation. The structure of the PapD-PapK complex also suggests that during pilus biogenesis, every subunit completes the immunoglobulin-like fold of its neighboring subunit via a mechanism termed donor strand exchange.

1 Department of Molecular Microbiology,
2 Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110, USA.
*   These authors contributed equally to this report.

dagger    To whom correspondence should be addressed.


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