Structural determinants underlying high-temperature adaptation of thermophilic xylanase from hot-spring microorganisms
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,...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2023-07-01
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| Series: | Frontiers in Microbiology |
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fmicb.2023.1210420/full |
| _version_ | 1797785234245156864 |
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| author | Yi Li Yi Li Yi Li Yi Li Hong-Qian Peng Li-Quan Yang Li-Quan Yang |
| author_facet | Yi Li Yi Li Yi Li Yi Li Hong-Qian Peng Li-Quan Yang Li-Quan Yang |
| author_sort | Yi Li |
| collection | DOAJ |
| description | 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. |
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| format | Article |
| id | doaj.art-538f6ad0bdaa4304b49923ec61c53d21 |
| institution | Directory Open Access Journal |
| issn | 1664-302X |
| language | English |
| last_indexed | 2024-03-13T00:51:11Z |
| publishDate | 2023-07-01 |
| publisher | Frontiers Media S.A. |
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| series | Frontiers in Microbiology |
| spelling | doaj.art-538f6ad0bdaa4304b49923ec61c53d212023-07-07T13:02:22ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2023-07-011410.3389/fmicb.2023.12104201210420Structural determinants underlying high-temperature adaptation of thermophilic xylanase from hot-spring microorganismsYi Li0Yi Li1Yi Li2Yi Li3Hong-Qian Peng4Li-Quan Yang5Li-Quan Yang6College of Mathematics and Computer Science, Dali University, Dali, ChinaCollege of Agriculture and Biological Science, Dali University, Dali, ChinaKey Laboratory of Bioinformatics and Computational Biology, Department of Education of Yunnan Province, Dali University, Dali, ChinaState Key Laboratory for Conservation and Utilization of Bio-Resource in Yunnan, Yunnan University, Kunming, ChinaCollege of Mathematics and Computer Science, Dali University, Dali, ChinaCollege of Agriculture and Biological Science, Dali University, Dali, ChinaKey Laboratory of Bioinformatics and Computational Biology, Department of Education of Yunnan Province, Dali University, Dali, ChinaThermophilic 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.https://www.frontiersin.org/articles/10.3389/fmicb.2023.1210420/fullxylanasehigh-temperature adaptationstructural determinantshot-spring microorganismsprotein dynamics |
| spellingShingle | Yi Li Yi Li Yi Li Yi Li Hong-Qian Peng Li-Quan Yang Li-Quan Yang Structural determinants underlying high-temperature adaptation of thermophilic xylanase from hot-spring microorganisms Frontiers in Microbiology xylanase high-temperature adaptation structural determinants hot-spring microorganisms protein dynamics |
| title | Structural determinants underlying high-temperature adaptation of thermophilic xylanase from hot-spring microorganisms |
| title_full | Structural determinants underlying high-temperature adaptation of thermophilic xylanase from hot-spring microorganisms |
| title_fullStr | Structural determinants underlying high-temperature adaptation of thermophilic xylanase from hot-spring microorganisms |
| title_full_unstemmed | Structural determinants underlying high-temperature adaptation of thermophilic xylanase from hot-spring microorganisms |
| title_short | Structural determinants underlying high-temperature adaptation of thermophilic xylanase from hot-spring microorganisms |
| title_sort | structural determinants underlying high temperature adaptation of thermophilic xylanase from hot spring microorganisms |
| topic | xylanase high-temperature adaptation structural determinants hot-spring microorganisms protein dynamics |
| url | https://www.frontiersin.org/articles/10.3389/fmicb.2023.1210420/full |
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