Crystal structure of polysaccharide lyase family 20 endo-β-1,4-glucuronan lyase from the filamentous fungus Trichoderma reesei
Crystal structure of polysaccharide lyase family 20 endo-β-1,4-glucuronan lyase from the filamentous fungus Trichoderma reesei
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DOI：
10.1016/j.febslet.2009.03.034
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发表时间：
2009-04-17
期刊：
影响因子：
3.5
通讯作者：
Isogai, Akira
中科院分区：
文献类型：
--
作者：
Konno, Naotake;Ishida, Takuya;Isogai, Akira
里氏木霉(Trichoderma Reesei)内切-β-(1-gt；4)-葡糖醛酸裂解酶(TrGL)的晶体结构为多糖裂解酶(PL)家族20的第一个三维结构，分辨率为1.8埃。TrGL具有典型的β-凝胶卷曲，类似于糖苷水解酶家族16和PL7酶。钙离子结合在远离裂隙的部位，似乎有助于稳定。裂隙中有几个完全保守的残基。根据与PL7海藻酸裂解酶A1-II‘的结构比较，预测了可能的催化残基。(C)2009年欧洲生化学会联合会。爱思唯尔出版，版权所有。
The crystal structure of endo-beta-(1 -> 4)-glucuronan lyase from Trichoderma reesei (TrGL) has been determined at 1.8 angstrom resolution as the first three-dimensional structure of polysaccharide lyase (PL) family 20. TrGL has a typical beta-jelly roll fold, which is similar to glycoside hydrolase family 16 and PL7 enzymes. A calcium ion is bound to the site far from the cleft and appears to contribute to the stability. There are several completely conserved residues in the cleft. Possible catalytic residues are predicted based on structural comparison with PL7 alginate lyase A1-II'. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.