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首页> 外文期刊>International Journal of Biological Macromolecules: Structure, Function and Interactions >Low-resolution SAXS and comparative modeling based structure analysis of endo-beta-1,4-xylanase a family 10 glycoside hydrolase from Pseudopedobacter saltans comb. nov
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Low-resolution SAXS and comparative modeling based structure analysis of endo-beta-1,4-xylanase a family 10 glycoside hydrolase from Pseudopedobacter saltans comb. nov

机译：基于低分辨率的肠胃蛋白酶10糖苷水解酶的低分辨率淋巴和基于比较的结构分析。 11月

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摘要

The structure and biophysical properties of endo beta-1,4-xylanase (PsGH10A) of family 10 glycoside hydrolase were characterized. The modeled PsGH10A structure showed classical (beta/alpha)(beta)-barrel fold. Ramachandran plot displayed 99.1% residues in favored and 0.3% in the generously allowed region and only 0.6% residues in disallowed region. The secondary structure analysis of PsGH10A by CD revealed 31.75% alpha-helices 20.0% beta-strands and 48.25% random coils. Protein melting study of PsGH10A showed complete unfolding at 60 degrees C and did not require any metal ion for its stability. Structural superposition and docking analysis confirmed the involvement of Glu156 and Glu263 residues in catalysis. SAXS analysis displayed that PsGH10A is monomeric in nature showing fully folded state in solution form. Guinier analysis gave the radius of gyration (Rg) 2.23-2.29 nm. Kratky plot indicated that the protein is fully folded globular shaped and flexible in solution form. The ab initio derived dummy model of PsGH10A displayed chicken thigh like shape. The ab initio derived dummy model superposed well with its comparative modeled structure except the N-terminal His-tag region. (C) 2018 Elsevier B.V. All rights reserved.
机译：胎儿10种糖苷水解酶的endoβ-1,4-木聚糖酶（PSGH10A）的结构和生物物理性质的特征在于。所建模的PSGH10A结构显示古典（β/α）（β）-Barrel折叠。 Ramachandran绘图显示99.1％的残留物，在慷慨的区域中有青睐和0.3％，并且在不允许的区域中仅为0.6％残基。 CD的PSGH10A的二次结构分析显示31.75％α-螺旋20.0％β-股和48.25％无随机线圈。 PSGH10A的蛋白质熔化研究显示在60摄氏度下完全展开，并且不需要任何金属离子的稳定性。结构叠加和对接分析证实了Glu156和Glu263残基在催化中的参与。 SAXS分析显示PSGH10A是性质中的单体，显示出溶液形式的完全折叠状态。 Guinier分析给出了旋转半径（RG）2.23-2.29 nm。 Kratky绘图表明，蛋白质完全折叠球形，柔性溶液形式。 PSGH10A的AB Initio衍生的伪模型显示了像形状的鸡大腿。除了N末端HIS标签区域之外，AB Initio衍生的虚设模型与其对比建模结构叠加。 （c）2018年elestvier b.v.保留所有权利。

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