Shape evolution with temperature of a thermotolerant protein (PeaT1) in solution detected by small angle X‐ray scattering
Shape evolution with temperature of a thermotolerant protein (PeaT1) in solution detected by small angle X‐ray scattering
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DOI：
10.1002/prot.24162
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发表时间：
2013-01
期刊：
影响因子：
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通讯作者：
Xue-qing Xing;Quan Liu;W. Wang;Kunhao Zhang;Tang Li;Q. Cai;G. Mo;Weidong Cheng;Dehong Wang
中科院分区：
文献类型：
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作者：
Xue-qing Xing;Quan Liu;W. Wang;Kunhao Zhang;Tang Li;Q. Cai;G. Mo;Weidong Cheng;Dehong Wang
来自细链格孢 (Alternaria tenuissima) (PeaT1) 的蛋白质引发子表现出优异的耐热性和作为农药在农业中的潜在应用。之前的同步辐射圆二色性研究表明，PeaT1蛋白的二级结构随着温度的变化是可逆的。为了进一步阐明其耐热性机制，本文采用同步辐射小角X射线散射（SAXS）技术研究了PeaT1蛋白的形状随温度的变化。基于 SAXS 数据的从头算结构恢复表明 PeaT1 蛋白具有长长形状，其 P2 对称轴沿长长不等轴方向。随着温度的升高，可以发现鹅颈花瓶状（25°C），到壶状（55°C），然后到椭圆形（85°C）的形状变化，并且这些形状变化也随着温度的降低而近似可逆。 PeaT1蛋白含有两个同源分子，每个分子均由F、NAC、T和UBA结构域组成。预测了四个域的结构。使用模拟退火算法将域结构叠加到 SAXS 形状上。结果发现，所有的结构域都随着温度的变化而发生位置旋转和平移，但NAC域相对稳定，起到框架的作用。这种形状变化信息为进一步探索其生物学功能和应用提供了线索。蛋白质 2013。© 2012 Wiley periodicals, Inc.
The protein elicitor from Alternaria tenuissima (PeaT1) presented excellent thermotolerance and potential application in agriculture as a pesticide. Previous synchrotron radiation circular dichroism study demonstrated that the secondary structures in PeaT1 protein are reversible with temperature change. To further clarify the mechanism of its thermotolerance, synchrotron radiation small angle x‐ray scattering (SAXS) technique was used to study the shape change of PeaT1 protein with temperature in this article. Ab initio structure restorations based on the SAXS data revealed that PeaT1 protein has a prolate shape with a P2 symmetry axis along the prolate anisometric direction. With temperature increase, a gooseneck vase‐like (25°C), to jug‐like (55°C), then to oval (85°C) shape change can be found, and these shape changes are also approximately reversible with temperature decrease. PeaT1 protein contains two homogenous molecules, and each of them consists of F, NAC, T, and UBA domains. The structures of the four domains were predicted. Simulated annealing algorithm was used to superimpose the domain structures onto the SAXS shapes. It was found that all the structural domains have position rotation and translation with temperature change, but the NAC domains are relatively stable, playing a role of frame. This shape change information provides clues for further exploring its biological function and application. Proteins 2013. © 2012 Wiley Periodicals, Inc.