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Science 13 August 1999: Vol. 285. no. 5430, pp. 1058 - 1061 DOI: 10.1126/science.285.5430.1058
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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,
1
Gabriel Waksman
2
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 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.
To whom correspondence should be addressed.
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