1PDK

PAPD-PAPK CHAPERONE-PILUS SUBUNIT COMPLEX FROM E.COLI P PILUS

Summary for 1PDK

• Entry DOI: 10.2210/pdb1pdk/pdb
• Descriptor: PROTEIN (CHAPERONE PROTEIN PAPD), PROTEIN (PROTEIN PAPK) (3 entities in total)
• Functional Keywords: chaperone, pilus, bacterial adhesion
• Biological source: Escherichia coli; More
• Cellular location: Periplasm: P15319; Secreted: P62532
• Total number of polymer chains: 2
• Total formula weight: 41454.93

Authors

Fuetterer, K.,Sauer, F.G.,Hultgren, S.J.,Waksman, G. (deposition date: 1999-03-29, release date: 1999-08-17, Last modification date: 2024-10-30)

Primary citation

Sauer, F.G.,Futterer, K.,Pinkner, J.S.,Dodson, K.W.,Hultgren, S.J.,Waksman, G.
Structural basis of chaperone function and pilus biogenesis.
Science, 285:1058-1061, 1999

PubMed 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.

PubMed: 10446050
DOI: 10.1126/science.285.5430.1058

Experimental method

X-RAY DIFFRACTION (2.4 Å)