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首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >Crystallization and preliminary crystallographic analysis of Abp, a GH27 beta-L-arabinopyranosidase from Geobacillus stearothermophilus
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Crystallization and preliminary crystallographic analysis of Abp, a GH27 beta-L-arabinopyranosidase from Geobacillus stearothermophilus

机译：嗜热地热芽孢杆菌GH27β-L-阿拉伯吡喃糖苷酶Abp的结晶和初步晶体学分析

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摘要

Geobacillus stearothermophilus T-6 is a thermophilic soil bacterium that possesses an extensive system for the utilization of hemicellulose. The bacterium produces a small number of endo-acting extracellular enzymes that cleave high-molecular-weight hemicellulolytic polymers into short decorated oligosaccharides, which are further hydrolysed into the respective sugar monomers by a battery of intracellular glycoside hydrolases. One of these intracellular processing enzymes is beta-L-arabinopyranosidase (Abp), which is capable of removing beta-L-arabinopyranose residues from naturally occurring arabinopolysaccharides. As arabino-polymers constitute a significant part of the hemicellulolytic content of plant biomass, their efficient enzymatic degradation presents an important challenge for many potential biotechnological applications. This aspect has led to an increasing interest in the biochemical characterization and structural analysis of this and related hemicellulases. Abp from G. stearothermophilus T-6 has recently been cloned, overexpressed, purified, biochemically characterized and crystallized in our laboratory, as part of its complete structure-function study. The best crystals obtained for this enzyme belonged to the primitive orthorhombic space group P2(1)2(1)2(1), with average unit-cell parameters a = 107.7, b = 202.2, c = 287.3 angstrom. Full diffraction data sets to 2.3 angstrom resolution have been collected for both the wild-type enzyme and its D197A catalytic mutant from flash-cooled crystals at 100 K, using synchrotron radiation. These data are currently being used for a high-resolution three-dimensional structure determination of Abp.
机译：嗜热脂肪热土芽孢杆菌T-6是嗜热土壤细菌，拥有广泛的利用半纤维素的系统。该细菌产生少量内切作用的细胞外酶，这些酶将高分子量的半纤维素分解聚合物切割成短修饰的寡糖，然后通过一系列细胞内糖苷水解酶将其进一步水解成相应的糖单体。这些细胞内加工酶之一是β-L-阿拉伯吡喃糖苷酶（Abp），其能够从天然存在的阿拉伯多糖中去除β-L-阿拉伯吡喃糖残基。由于阿拉伯聚合物构成植物生物质的半纤维素分解含量的重要组成部分，其有效的酶促降解对许多潜在的生物技术应用提出了重要的挑战。该方面已引起对该半纤维素酶和相关半纤维素酶的生物化学表征和结构分析的日益增长的兴趣。作为完整结构功能研究的一部分，最近在我们的实验室中克隆了嗜热脂肪热菌T-6的Abp，对其进行了过表达，纯化，生物化学表征和结晶。对该酶获得的最佳晶体属于原始正交空间群P2（1）2（1）2（1），平均晶胞参数a = 107.7，b = 202.2，c = 287.3埃。使用同步加速器辐射，已从100 K的快速冷却晶体中收集了野生型酶及其D197A催化突变体的全部衍射数据，分辨率为2.3埃。这些数据当前用于Abp的高分辨率三维结构确定。

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