1n0l
From Proteopedia
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Crystal structure of the PapD chaperone (C-terminally 6x histidine-tagged) bound to the PapE pilus subunit (N-terminal-deleted) from uropathogenic E. coli
Overview
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.
About this Structure
1N0L is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Chaperone priming of pilus subunits facilitates a topological transition that drives fiber formation., Sauer FG, Pinkner JS, Waksman G, Hultgren SJ, Cell. 2002 Nov 15;111(4):543-51. PMID:12437927
Page seeded by OCA on Tue Nov 20 21:51:22 2007
