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Internet Electronic Journal of Molecular Design - IEJMD, ISSN 1538-6414, CODEN IEJMAT
ABSTRACT - Internet Electron. J. Mol. Des. December 2003, Volume 2, Number 12, 835-851

Structural Contributions for Thermostability of a New Endo-1,4-β-xylanase from the Fungus Humicola grisea
Sonia M. De Freitas, Werner L. Treptow, Fabricia P. De Faria, Maristela De O. Azevedo, and Bernard Maigret
Internet Electron. J. Mol. Des. 2003, 2, 835-851

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Abstract:
The Humicola grisea var. thermoidea is known as a good producer of hydrolytic enzymes. The H. grisea endo-1,4-β-xylanase gene (xyn2) was isolated and its sequence was translated into a predicted protein coding for a xylanase of 23 kDa. A structural model of H. grisea endo-1,4-β-xylanase (XYN2) was built by homology modeling based on the database search results of related proteins, belonging to Glycoside Hydrolase Family 11 (GH11). The inactive/active conformation transition of the XYN2 model active site is pH sensitive as revealed by independent molecular dynamics simulations at different pH. The active conformation exhibits the common structural β-sheet twisted architecture of the GH11. The active site is formed by a large cleft containing the catalytic residues (E84 and E175), and is stabilized by hydrogen bond network involving the Q134, Y75, Y88, W77, and Y169. Additionally, the structural properties described by the model explain the observed thermostability of the XYN2 protein. According to our results, the thermostability of XYN2 protein, compared to mesophilic xylanases, can be explained by an additional electrostatic network and extra aromatic exposed residues.

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