Structural determinants underlying high-temperature adaptation of thermophilic xylanase from hot-spring microorganisms.

ABSTRACT: Thermophilic xylanases from hot-spring microorganisms play potential biological and industrial applications for renewable and sustainable social development. However, high-temperature adaptation mechanisms of these thermophilic xylanases remain elusive at the molecular and evolutionary levels. Here, two recently reported xylanases, named XynDRTY1 and XynM1, from hot springs were subjected to molecular dynamics (MD) simulations at a series of temperature gradients and comparatively analyzed in comparison with the evolutionary background of the xylanase family. Comparative analysis of MD trajectories revealed that the XynM1 exhibits smaller structural dynamics and greater thermal stability than the XynDRTY1, although both share a similar fold architecture with structural differences in the β

SUBMITTER: Li Y 

PROVIDER: S-EPMC10360402 | biostudies-literature | 2023

REPOSITORIES: biostudies-literature