Structural basis and mechanism of the unfolding-induced activation of HdeA, a bacterial acid response chaperone
Abstract
The role of protein structural disorder in biological functions has gained increasing attention in the past decade. The bacterial acid-resistant chaperone HdeA belongs to a group of “conditionally disordered” proteins, because it is inactive in its well-structured state and becomes activated via an order-to-disorder transition under acid stress. However, the mechanism for unfolding-induced activation remains unclear because of a lack of...
Paper Details
Title
Structural basis and mechanism of the unfolding-induced activation of HdeA, a bacterial acid response chaperone
Published Date
Mar 1, 2019
Volume
294
Issue
9
Pages
3192 - 3206
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