Structural basis of chaperone function and pilus biogenesis

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

Research output: Contribution to journalArticlepeer-review

326 Scopus citations

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 g.4 angstrom resolution, reveals that the chaperone functions by donating its G1 β 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.

Original languageEnglish
Pages (from-to)1058-1061
Number of pages4
JournalScience
Volume285
Issue number5430
DOIs
StatePublished - Aug 13 1999

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