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

Yi Li; Hong-Qian Peng; Li-Quan Yang

doi:10.3389/fmicb.2023.1210420

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

Front Microbiol. 2023 Jul 7:14:1210420. doi: 10.3389/fmicb.2023.1210420. eCollection 2023.

Authors

Yi Li^{1

2

3

4}, Hong-Qian Peng¹, Li-Quan Yang^{2

3}

Affiliations

¹ College of Mathematics and Computer Science, Dali University, Dali, China.
² College of Agriculture and Biological Science, Dali University, Dali, China.
³ Key Laboratory of Bioinformatics and Computational Biology, Department of Education of Yunnan Province, Dali University, Dali, China.
⁴ State Key Laboratory for Conservation and Utilization of Bio-Resource in Yunnan, Yunnan University, Kunming, China.

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 βα_loops. Local regions whose conformational flexibility and regular secondary structure exhibited differences as temperature increases were closely related to the high-temperature adaptation of xylanase, implying that stabilization of these regions is a feasible strategy to improve the thermal stability of xylanases. Furthermore, coevolutionary information from the xylanase family further specified the structural basis of xylanases. Thanks to these results about the sequence, structure, and dynamics of thermophilic xylanases from hot springs, a series of high-temperature-related structural determinants were resolved to promote understanding of the molecular mechanism of xylanase high-temperature adaptation and to provide direct assistance in the improvement of xylanase thermal stability.

Keywords: high-temperature adaptation; hot-spring microorganisms; protein dynamics; structural determinants; xylanase.