Structural model for family 32 of glycosyl-hydrolase enzymes
Structural model for family 32 of glycosyl-hydrolase enzymes
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DOI：
10.1002/(sici)1097-0134(19981115)33:3
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发表时间：
1998-11-15
期刊：
影响因子：
--
通讯作者：
Valencia, A
中科院分区：
文献类型：
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作者：
Pons, T;Olmea, O;Valencia, A
提出了一个基于β-螺旋桨折叠的糖基水解酶家族32的结构模型。该模型是由TOPITS和THREADER两种不同的穿线方法共同预测得出的。此外，我们还使用了活性中心残基的相关突变分析和预测来验证所提出的模型。物理技术(圆二色谱和差示扫描量热法)证实了预测的两个方面，即所提出的全贝塔折叠和多域结构。以神经氨酸酶(1nscA)的结构为模板，得到最可靠的三维模型。该模型中活性中心残基位置的分析与Reddy和Maley(J，Biol)提出的催化机理相一致。该序列含有天冬氨酸、谷氨酸和半胱氨酸三个保守残基。基于这一分析，我们提出了另一个保守残基(Asp 162)参与了催化机理。该模型将有助于进一步研究糖基水解酶家族32的物理和生化特性，蛋白质33：383-395,1998，(C)1998 Wiley-Liss，Inc.
A structural model is presented for family 32 of the glycosyl-hydrolase enzymes based on the beta-propeller fold. The model is derived from the common prediction of two different threading methods, TOPITS and THREADER. In addition, we used a correlated mutation analysis and prediction of active-site residues to corroborate the proposed model. Physical techniques (circular dichroism and differential scanning calorimetry) confirmed two aspects of the prediction, the proposed all-beta fold and the multi-domain structure. The most reliable three-dimensional model was obtained using the structure of neuraminidase (1nscA) as template. The analysis of the position of the active site residues in this model is compatible with the catalytic mechanism proposed by Reddy and Maley (J, Biol. Chem, 271:13953-13958, 1996), which includes three conserved residues, Asp, Glu, and Cys. Based on this analysis, we propose the participation of one more conserved residue (Asp 162) in the catalytic mechanism. The model will facilitate further studies of the physical and biochemical characteristics of family 32 of the glycosyl-hydrolases, Proteins 33:383-395, 1998, (C) 1998 Wiley-Liss,Inc.