CRYSTAL-STRUCTURE OF GLUCOSE-OXIDASE FROM ASPERGILLUS-NIGER REFINED AT 2 .3 ANGSTROM RESOLUTION
CRYSTAL-STRUCTURE OF GLUCOSE-OXIDASE FROM ASPERGILLUS-NIGER REFINED AT 2 .3 ANGSTROM RESOLUTION
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DOI：
10.1006/jmbi.1993.1015
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发表时间：
1993-01-05
影响因子：
5.6
通讯作者：
SCHOMBURG, D
中科院分区：
文献类型：
--
作者：
HECHT, HJ;KALISZ, HM;SCHOMBURG, D
葡萄糖氧化酶（β-d-葡萄糖：氧1-氧化还原酶，EC 1.1.3.4）是一种依赖fad的酶，它催化分子氧氧化β-d-葡萄糖。用同形置换法测定了尼日利亚曲霉部分去糖基化酶的晶体结构，并将其细化到2·3 Å分辨率。在10·0 ~ 2·3 Å分辨率范围内的反射，最终晶体学icr值为18.1%。精化模型包括580个氨基酸残基、FAD辅因子、6 -乙酰氨基葡萄糖残基、3个甘露糖残基和152个溶剂分子。fad结合域在拓扑结构上与其他fad结合蛋白非常相似。底物结合结构域由非连续的序列片段形成，其特征是深口袋。该口袋的一侧由反平行的六链β片组成，另一侧口袋底部的FAD黄素环系统。活性位点口袋的部分入口位于二聚体酶的第二亚基的界面上，由20个残基盖形成，该盖还覆盖了部分fad结合位点。附着在Asn89顶部的碳水化合物部分形成了二聚体亚基之间的连接。
Glucose oxidase (β-d-glucose: oxygen 1-oxidoreductase, EC 1.1.3.4) is an FAD-dependent enzyme that catalyzes the oxidation of β-d-glucose by molecular oxygen. The crystal structure of the partially deglycosylated enzyme fromAspergillus nigerhas been determined by isomorphous replacement and refined to 2·3 Å resolution. The final crystallographicR-value is 18·1% for reflections between 10·0 and 2·3 Å resolution. The refined model includes 580 amino acid residues, the FAD cofactor, sixN-acetylglucosamine residues, three mannose residues and 152 solvent molecules. The FAD-binding domain is topologically very similar to other FAD-binding proteins. The substrate-binding domain is formed from non-continuous segments of sequence and is characterized by a deep pocket. One side of this pocket is formed by a six-stranded antiparallel β-sheet with the flavin ring system of FAD located at the bottom of the pocket on the opposite side. Part of the entrance to the active site pocket is at the interface to the second subunit of the dimeric enzyme and is formed by a 20-residue lid, which in addition covers parts of the FAD-binding site. The carbohydrate moiety attached to Asn89 at the tip of this lid forms a link between the subunits of the dimer.