1pdk
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PAPD-PAPK CHAPERONE-PILUS SUBUNIT COMPLEX FROM E.COLI P PILUS
OverviewOverview
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.
About this StructureAbout this Structure
1PDK is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis of chaperone function and pilus biogenesis., Sauer FG, Futterer K, Pinkner JS, Dodson KW, Hultgren SJ, Waksman G, Science. 1999 Aug 13;285(5430):1058-61. PMID:10446050
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