Pushed to extremes: distinct effects of high temperature vs. pressure on the structure of an atypical phosphatase.

ABSTRACT: Protein function hinges on small shifts of three-dimensional structure. Elevating temperature or pressure may provide experimentally accessible insights into such shifts, but the effects of these distinct perturbations on protein structures have not been compared in atomic detail. To quantitatively explore these two axes, we report the first pair of structures at physiological temperature vs. high pressure for the same protein, STEP (PTPN5). We show that these perturbations have distinct and surprising effects on protein volume, patterns of ordered solvent, and local backbone and side-chain conformations. This includes novel interactions between key catalytic loops only at physiological temperature, and a distinct conformational ensemble for another active-site loop only at high pressure.

SUBMITTER: Guerrero L 

PROVIDER: S-EPMC10187168 | biostudies-literature | 2023 May

REPOSITORIES: biostudies-literature