8KEU
Crystal Structures of Endo-beta-1,4-xylanase II mutant T2CT28C
Summary for 8KEU
| Entry DOI | 10.2210/pdb8keu/pdb |
| Descriptor | Endo-1,4-beta-xylanase II, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, IODIDE ION, ... (4 entities in total) |
| Functional Keywords | endo-beta-1, 4-xylanase, hydrolase |
| Biological source | Trichoderma reesei |
| Total number of polymer chains | 1 |
| Total formula weight | 21589.68 |
| Authors | |
| Primary citation | Li, Z.,Li, X.,Zhou, Y.,Lu, M.,Li, M.,Zhu, Y.,Wan, Q. Rational design of GH11 xylanase to balance the activity-stability trade-off. Int.J.Biol.Macromol., 311:143063-143063, 2025 Cited by PubMed Abstract: Enhancements of enzyme stability often compromise activity; thus, achieving an optimal balance between stability and activity poses a significant challenge in enzyme engineering. Our study investigated the stability-activity trade-off using the GH11 xylanase XynII as a model. A rational design strategy integrating crystal structure analysis and molecular dynamics simulations was used to distinguish regions important for structural stability and catalytic activity. Structural stability and activity were significantly enhanced by the introduction of two disulfide bonds involving four residues (T2C/T28C/R81C/T168C), which conferred a 75 % increase in activity, a 12.1 °C increase in T, and an 80-fold improvement in half-life compared to the wild-type enzyme. The incorporation of two additional mutations (Q125A/I129S) was shown to increase the catalytic activity by 30 % by enhancing the dynamics of the active site. Our results illustrate a successful strategy for simultaneously increasing activity and stability by optimizing the dynamics of the catalytic region and the rigidity of the noncatalytic region. PubMed: 40253048DOI: 10.1016/j.ijbiomac.2025.143063 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.1 Å) |
Structure validation
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