Comparative analysis of thermal adaptations of extremophilic prolyl oligopeptidases.

ABSTRACT: Prolyl oligopeptidases from psychrophilic, mesophilic, and thermophilic organisms found in a range of natural environments are studied using a combination of protein structure prediction, atomistic molecular dynamics, and trajectory analysis to determine how the S9 protease family adapts to extreme thermal conditions. We compare our results with hypotheses from the literature regarding structural adaptations that allow proteins to maintain structure and function at extreme temperatures, and we find that, in the case of prolyl oligopeptidases, only a subset of proposed adaptations are employed for maintaining stability. The catalytic and propeller domains are highly structured, limiting the range of mutations that can be made to enhance hydrophobicity or form disulfide bonds without disrupt

SUBMITTER: Diessner EM 

PROVIDER: S-EPMC11427779 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature