Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sauer FG, Pinkner JS, Waksman G, Hultgren SJ. Chaperone priming of pilus subunits facilitates a topological transition that drives fiber formation. Cell. 2002 Nov 15;111(4):543-51. PMID:12437927
