Crystal structure of intracellular family 1 β‐glucosidase BGL1A from the basidiomycete Phanerochaete chrysosporium
Crystal structure of intracellular family 1 β‐glucosidase BGL1A from the basidiomycete Phanerochaete chrysosporium
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DOI：
10.1016/j.febslet.2007.03.009
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发表时间：
2007-04
期刊：
影响因子：
3.5
通讯作者：
Y. Nijikken;T. Tsukada;K. Igarashi;M. Samejima;T. Wakagi;H. Shoun;S. Fushinobu
中科院分区：
文献类型：
--
作者：
Y. Nijikken;T. Tsukada;K. Igarashi;M. Samejima;T. Wakagi;H. Shoun;S. Fushinobu
白腐真菌 Phanerochaete chrysosporium 具有两种属于糖苷水解酶 (GH) 家族 1 的细胞内 β-葡萄糖苷酶（BGL1A 和 BGL1B）。BGL1B 可以有效水解纤维二糖和纤维二酸内酯，但 BGL1A 不能。我们已经确定了无底物和葡萄糖酸内酯复合形式的 BGL1A 的晶体结构。亚位点-1（糖基位点）的整体结构和特征与其他已知的GH1酶相似。覆盖在(β/α)8桶上的环区域明显偏离，它们形成了BGL1A独特的亚位点+1（糖苷配基位点）。
The white-rot fungus Phanerochaete chrysosporium has two intracellular β-glucosidases (BGL1A and BGL1B) belonging to glycoside hydrolase (GH) family 1. BGL1B effectively hydrolyzes cellobiose and cellobionolactone, but BGL1A does not. We have determined the crystal structure of BGL1A in substrate-free and gluconolactone complexed forms. The overall structure and the characteristic of subsite −1 (glycone site) were similar to those of other known GH1 enzymes. The loop regions covering on the (β/α)8barrel was significantly deviated, and they form a unique subsite +1 (aglycone site) of BGL1A.