Article
Unique residues involved in activation of the multitasking protease/chaperone HtrA from Chlamydia trachomatis.
PloS one - 1 Jan 2011
Huston Wilhelmina M, Tyndall Joel D A, Lott William B, Stansfield Scott H, Timms Peter
Abstract excerpt
DegP, a member of the HtrA family of proteins, conducts critical bacterial protein quality control by both chaperone and proteolysis activities. The regulatory mechanisms controlling these two distinct activities, however, are unknown. DegP activation is known to involve a unique mechanism of allosteric binding, conformational changes and oligomer formation. We have uncovered a novel role for the residues at the...
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