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 experimental information on the unfolded state conformation and the chaperone-client interactions. Herein, we used advanced solution NMR methods to characterize the activated-state conformation of HdeA under acidic conditions and identify its client-binding sites. We observed that the structure of activated HdeA becomes largely disordered and exposes two hy

SUBMITTER: Yu XC 

PROVIDER: S-EPMC6398119 | biostudies-literature | 2019 Mar

REPOSITORIES: biostudies-literature