8YJJ

Crystal structure of xylanase from Trichoderma longibrachiatum

Summary for 8YJJ

• Entry DOI: 10.2210/pdb8yjj/pdb
• Descriptor: Endo-1,4-beta-xylanase (2 entities in total)
• Functional Keywords: room temperature, xylanase, trichoderma longibrachiatum, hydrolase
• Biological source: Trichoderma longibrachiatum
• Total number of polymer chains: 1
• Total formula weight: 20838.44

Authors

Nam, K.H. (deposition date: 2024-03-02, release date: 2024-03-13, Last modification date: 2024-10-16)

Primary citation

Nam, K.H.
Temperature-dependent structural changes in xylanase II from Trichoderma longibrachiatum.
Carbohydr.Res., 541:109173-109173, 2024

PubMed 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 (TloXynII) showed a B-factor value 2.09 times higher than that of the cryogenic-temperature structure of TloXynII (TloXynII). Subtle movement of the catalytic and substrate binding residues was observed between TloXynII and TloXynII. In TloXynII, the thumb domain exhibited high flexibility, whereas in TloXynII, the finger domain exhibited high flexibility. The substrate binding cleft of TloXynII was narrower than that of TloXynII, indicating a distinct finger domain conformation. Numerous water molecule networks were observed in the substrate binding cleft of TloXynII, whereas only a few water molecules were observed in TloXynII. These structural analyses expand our understanding of the temperature-dependent conformational changes in xylanase.

PubMed: 38833820
DOI: 10.1016/j.carres.2024.109173

Experimental method

X-RAY DIFFRACTION (1.9 Å)