Crystal structure and thermodynamic dissection of chitin oligosaccharide binding to the LysM module of chitinase-A from Pteris ryukyuensis
Crystal structure and thermodynamic dissection of chitin oligosaccharide binding to the LysM module of chitinase-A from Pteris ryukyuensis
复制标题
琉球凤尾几丁质酶-A LysM 模块结合的几丁质寡糖的晶体结构和热力学解析
DOI：
10.1016/j.bbrc.2017.08.143
复制
发表时间：
2017
期刊：
影响因子：
--
通讯作者：
T.
中科院分区：
文献类型：
--
作者：
Ohnuma;T.;Taira;T.;Umemoto;N.;Kitaoku;Y.;Sørlie;M.;Numata;T. and Fukamizo;T.
我们从mpterisryukyuensischitinase - a （PrLysM2）中测定了LysM模块的晶体结构，分辨率为1.8 Å。prlysm2的结构和结合分析表明，该模块识别分子一侧由五个糖结合亚位组成的浅槽中的几丁质寡糖。通过ITC测定（GlcNAc）6、（GlcNAc）5和（GlcNAc）4toPrLysM2结合的自由能变化（ΔGr°）分别为−5.4、−5、4和−4.6 kcal mol−1。对（GlcNAc）6的结合能进行热力学分析，发现其动力是焓变（ΔHr°=−11.7±0.2 kcal/mol）和溶剂化熵变（−TΔSsolv°=−5.9±0.6 kcal/mol）。这是第一次描述甲壳素寡糖结合LysM模块的热力学特征。
We determined the crystal structure of a LysM module fromPterisryukyuensischitinase-A (PrLysM2) at a resolution of 1.8 Å. Structural and binding analysis ofPrLysM2 indicated that this module recognizes chitin oligosaccharides in a shallow groove comprised of five sugar-binding subsites on one side of the molecule. The free energy changes (ΔGr°) for binding of (GlcNAc)6, (GlcNAc)5, and (GlcNAc)4toPrLysM2 were determined to be −5.4, −5,4 and −4.6 kcal mol−1, respectively, by ITC. Thermodynamic dissection of the binding energetics of (GlcNAc)6revealed that the driving force is the enthalpy change (ΔHr° = −11.7 ± 0.2 kcal/mol) and the solvation entropy change (−TΔSsolv° = −5.9 ± 0.6 kcal/mol). This is the first description of thermodynamic signatures of a chitin oligosaccharide binding to a LysM module.