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Temperature-dependent structural changes in xylanase II from Trichoderma longibrachiatum.
- Source :
-
Carbohydrate Research . Jul2024, Vol. 541, pN.PAG-N.PAG. 1p. - Publication Year :
- 2024
-
Abstract
- Endo-β-1,4-xylanases degrade heteroxylans that constitute the lignocellulosic plant cell wall. This enzyme is widely used in the food, paper, textile, and biorefinery industries. Temperature affects the optimum activity of xylanase and is an important factor in its application. Various structural analyses of xylanase have been performed, but its structural influence by temperature is not fully elucidated. To better understand the structural influence of xylanase due to temperature, the crystal structure of xylanase II from Trichoderma longibrachiatum (TloXynII) at room and cryogenic temperatures was determined at 2.1 and 1.9 Å resolution, respectively. The room-temperature structure of TloXynII (TloXynIIRT) showed a B-factor value 2.09 times higher than that of the cryogenic-temperature structure of TloXynII (TloXynIICryo). Subtle movement of the catalytic and substrate binding residues was observed between TloXynIIRT and TloXynIICryo. In TloXynIIRT, the thumb domain exhibited high flexibility, whereas in TloXynIICryo, the finger domain exhibited high flexibility. The substrate binding cleft of TloXynIIRT was narrower than that of TloXynIICryo, indicating a distinct finger domain conformation. Numerous water molecule networks were observed in the substrate binding cleft of TloXynIICryo, whereas only a few water molecules were observed in TloXynIIRT. These structural analyses expand our understanding of the temperature-dependent conformational changes in xylanase. [Display omitted] • The crystal structures of TloXynII at room and cryogenic temperatures were determined. • TloXynIIRT and TloXynIICryo exhibited different conformations for the catalytic and substrate-binding residues. • The substrate-binding cleft of TloXynIIRT was narrower than that of TloXynIICryo. • TloXynIIRT showed a B-factor value that was 2.09 times higher than that of TloXynIICryo. • The regions of higher flexibility differed between TloXynIIRT and TloXynIICryo. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00086215
- Volume :
- 541
- Database :
- Academic Search Index
- Journal :
- Carbohydrate Research
- Publication Type :
- Academic Journal
- Accession number :
- 177844844
- Full Text :
- https://doi.org/10.1016/j.carres.2024.109173