β-Glucosidase from the thermophilic bacterium Caldicellulosiruptor saccharolyticus (Bgl1) has been denoted as having an attractive catalytic profile for various industrial applications. Bgl1 catalyses the final step of in the decomposition of cellulose, an unbranched glucose polymer that has attracted the attention of researchers in recent years as it is the most abundant renewable source of reduced carbon in the biosphere. With the aim of enhancing the thermostability of Bgl1 for a broad spectrum of biotechnological processes, it has been subjected to structural studies. Crystal structures of Bgl1 and its complex with glucose were determined at 1.47 and 1.95 Å resolution, respectively. Bgl1 is a member of glycosyl hydrolase family 1 (GH1 superfamily, EC 3.2.1.21) and the results showed that the 3D structure of Bgl1 follows the overall architecture of the GH1 family, with a classical (β/α)8 TIM-barrel fold. Comparisons of Bgl1 with sequence or structural homologues of β-glucosidase reveal quite similar structures but also unique structural features in Bgl1 with plausible functional roles.

中文翻译：

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来自嗜热细菌 Caldicellulosiruptor saccharolyticus 的 β-葡萄糖苷酶的结构研究。


来自嗜热细菌 Caldicellulosiruptor saccharolyticus (Bgl1) 的 β-葡萄糖苷酶已被认为对各种工业应用具有有吸引力的催化特性。 Bgl1 催化纤维素分解的最后一步，纤维素是一种无支链的葡萄糖聚合物，近年来引起了研究人员的关注，因为它是生物圈中最丰富的可再生碳还原来源。为了增强 Bgl1 在广泛生物技术过程中的热稳定性，对其进行了结构研究。 Bgl1 及其与葡萄糖的复合物的晶体结构分别以 1.47 和 1.95 Å 的分辨率测定。 Bgl1 是糖基水解酶家族 1（GH1 超家族，EC 3.2.1.21）的成员，结果表明 Bgl1 的 3D 结构遵循 GH1 家族的整体架构，具有经典的 (β/α)8 TIM 桶折叠。 Bgl1 与 β-葡萄糖苷酶的序列或结构同源物的比较揭示了 Bgl1 的结构非常相似，但也具有独特的结构特征，具有合理的功能作用。