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嗜热子囊菌主要内切葡聚糖酶的原子分辨率结构

Atomic resolution structure of the major endoglucanase from Thermoascus aurantiacus.

作者信息

Van Petegem F, Vandenberghe I, Bhat M K, Van Beeumen J

机构信息

Laboratorium voor Eiwitbiochemie en Eiwitengineering, Universiteit Gent, B-9000, Gent, Belgium.

出版信息

Biochem Biophys Res Commun. 2002 Aug 9;296(1):161-6. doi: 10.1016/s0006-291x(02)00775-1.

DOI:10.1016/s0006-291x(02)00775-1
PMID:12147244
Abstract

The crystal structure of the major endoglucanase from the thermophilic fungus Thermoascus aurantiacus was determined by single isomorphous replacement at 1.12A resolution. The full sequence supports the classification of the protein in a subgroup of glycoside hydrolase family 5 for which no structural data are available yet. The active site shows eight critical residues, strictly conserved within family 5. In addition, aromatic residues that line the substrate-binding cleft and that are possibly involved in substrate-binding are identified. A number of residues seem to be conserved among members of the subtype, including a disulphide bridge between Cys212 and Cys249.

摘要

嗜热真菌橙色嗜热子囊菌主要内切葡聚糖酶的晶体结构通过单对映体置换法在1.12埃分辨率下测定。完整序列支持将该蛋白质归类于糖苷水解酶家族5的一个亚组,目前该亚组尚无结构数据。活性位点显示出8个关键残基,在家族5中严格保守。此外,还鉴定出了位于底物结合裂隙内且可能参与底物结合的芳香族残基。一些残基似乎在该亚型成员中保守,包括Cys212和Cys249之间的二硫键。

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