1N0L

Crystal structure of the PapD chaperone (C-terminally 6x histidine-tagged) bound to the PapE pilus subunit (N-terminal-deleted) from uropathogenic E. coli

Summary for 1N0L

• Entry DOI: 10.2210/pdb1n0l/pdb
• Related: 1N12
• Descriptor: Chaperone protein PapD, mature Fimbrial protein PapE (3 entities in total)
• Functional Keywords: immunoglobulin-like fold, donor strand complemenation, donor strand exchange, chaperone priming, pilus fiber assembly, chaperone
• Biological source: Escherichia coli; More
• Cellular location: Periplasm: P15319; Secreted: P08407
• Total number of polymer chains: 4
• Total formula weight: 80783.00

Authors

Sauer, F.G.,Pinkner, J.S.,Waksman, G.,Hultgren, S.J. (deposition date: 2002-10-14, release date: 2002-12-11, Last modification date: 2024-11-20)

Primary citation

Sauer, F.G.,Pinkner, J.S.,Waksman, G.,Hultgren, S.J.
Chaperone priming of pilus subunits facilitates a topological transition that drives fiber formation
Cell(Cambridge,Mass.), 111:543-551, 2002

PubMed Abstract: Periplasmic chaperones direct the assembly of adhesive, multi-subunit pilus fibers that play critical roles in bacterial pathogenesis. Pilus assembly occurs via a donor strand exchange mechanism in which the N-terminal extension of one subunit replaces the chaperone G(1) strand that transiently occupies a groove in the neighboring subunit. Here, we show that the chaperone primes the subunit for assembly by holding the groove in an open, activated conformation. During donor strand exchange, the subunit undergoes a topological transition that triggers the closure of the groove and seals the N-terminal extension in place. It is this topological transition, made possible only by the priming action of the chaperone that drives subunit assembly into the fiber.

PubMed: 12437927
DOI: 10.1016/S0092-8674(02)01050-4

Experimental method

X-RAY DIFFRACTION (2.3 Å)