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- Title
Structural basis of chaperone function and pilus biogenesis.
- Authors
Sauer, F G; Fütterer, K; Pinkner, J S; Dodson, K W; Hultgren, S J; Waksman, G
- Abstract
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 G(1) 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.
- Publication
Science (New York, N.Y.), 1999, Vol 285, Issue 5430, p1058
- ISSN
0036-8075
- Publication type
Journal Article
- DOI
10.1126/science.285.5430.1058