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Atomic (0.94 A) resolution structure of an inverting glycosidase in complex with substrate.

机译:与底物复合的反向糖苷酶的原子(0.94 A)拆分结构。

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摘要

The crystal structure of Clostridium thermocellum endoglucanase CelA in complex with cellopentaose has been determined at 0.94 A resolution. The oligosaccharide occupies six D-glucosyl-binding subsites, three on either side of the scissile glycosidic linkage. The substrate and product of the reaction occupy different positions at the reducing end of the cleft, where an extended array of hydrogen-bonding interactions with water molecules fosters the departure of the leaving group. Severe torsional strain upon the bound substrate forces a distorted boat(2,5) B conformation for the glucosyl residue bound at subsite -1, which facilitates the formation of an oxocarbenium ion intermediate and might favor the breakage of the sugar ring concomitant with catalysis.
机译:热纤梭菌内切葡聚糖酶CelA与纤维戊糖复合的晶体结构已确定为0.94 A分辨率。寡糖占据六个D-葡萄糖基结合亚位点,在易裂糖苷键的任一侧上三个。反应的底物和产物在裂隙的还原端占据不同的位置,与水分子的氢键相互作用的扩展阵列促进了离去基团的离开。在结合的底物上的严重扭转应变迫使结合在亚位点-1上的葡糖残基扭曲的舟(2,5)B构象,这有利于氧羰基离子中间体的形成,并可能促进糖环的断裂,并伴随催化作用。

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