Solution scattering studies of conformation stability of xylanase XYNII from Trichoderma longibrachiatum
Solution scattering studies of conformation stability of xylanase XYNII from Trichoderma longibrachiatum
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DOI：
10.1002/bip.20531
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发表时间：
2006-09-01
期刊：
影响因子：
2.9
通讯作者：
Kozak, Maciej
中科院分区：
文献类型：
--
作者：
Kozak, Maciej
木聚糖酶（内切-1，4-β-木聚糖酶; EC 3.2.1.8）是催化木聚糖水解反应的酶。利用同步辐射小角和广角散射（SAXS-WAXS）技术研究了长枝木霉（Trichoderma longibrachoatum，原里氏木霉）木聚糖酶H（XYNII）分子在不同pH值下的结构。对表征木聚糖酶的回转半径的分析已经证实了上述酶结构的稳定性（回转半径从1.65至1.74 nm变化）。在SAXS数据的基础上，利用从头算方法和DALAI_GA和DAMMIN程序，对木聚糖酶分子在溶液中的低分辨结构进行了重构。将完整的SAXS-WAXS数据集（0.15 > s > 9.5 nm（-1））输入程序GASBOR，使我们能够构建木聚糖酶分子虚拟残基模型的链状空间分布。模型分子的形状与晶体中木聚糖酶分子的形状相似，并显示出使分子类似于右手的特征不对称性。(c)2006 Wiley Periodicals，Inc.
Xylanase (endo-1,4-beta-xylanase; EC 3.2.1.8) is an enzyme that catalyzes the hydrolysis reaction of xylan. The structure of the xylanase H (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. (c) 2006 Wiley Periodicals, Inc.