Solution scattering studies of conformation stability of xylanase XYNII from Trichoderma longibrachiatum

✍ Scribed by Maciej Kozak

• Book ID: 101722188
• Publisher: Wiley (John Wiley & Sons)
• Year: 2006
• Tongue: English
• Weight: 288 KB
• Volume: 83
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/bip.20531

✦ Synopsis

Abstract

Xylanase (endo‐1,4‐β‐xylanase; EC 3.2.1.8) is an enzyme that catalyzes the hydrolysis reaction of xylan. The structure of the xylanase II (XYNII) molecule from Trichoderma longibrachoatum (formerly Trichoderma reesei) in a solution and at different pH values has been studied by small‐ and wide‐angle scattering of synchrotron radiation (SAXS‐WAXS). Analysis of the radius of gyration that characterizes xylanase has confirmed the stability of the above enzyme structure (the radius of gyration varied from 1.65 to 1.74 nm). On the basis of the SAXS data, the low‐resolution structure of the xylanase molecule in solution has been reconstructed by using ab initio methods and programs DALAI_GA and DAMMIN. The full SAXS‐WAXS data set (0.15 > s > 9.5 nm^−1^) fed to the program GASBOR permitted us to construct a chain‐like spatial distribution of a dummy residues model of the xylanase molecule. The shape of the model molecules is similar to that of xylanase molecule in the crystal and shows the characteristic asymmetry that makes the molecule to resemble a right hand. © 2006 Wiley Periodicals, Inc. Biopolymers 83:95–102, 2006

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