Shape evolution with temperature of a thermotolerant protein (PeaT1) in solution detected by small angle X-ray scattering
文献类型: 外文期刊
第一作者: Wang, Wei
作者: Wang, Wei;Zhang, Kunhao;Cai, Quan;Mo, Guang;Cheng, Weidong;Wang, Dehong;Gong, Yu;Chen, Zhongjun;Wu, Zhonghua;Xing, Xueqing;Cheng, Weidong;Wang, Dehong;Gong, Yu;Wu, Zhonghua;Liu, Quan;Li, Tang;Qiu, Dewen;Liu, Quan
作者机构:
关键词: Domain;PeaT1;SAXS;SRCD;Structure prediction;Structure restoration
期刊名称:PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS ( 影响因子:3.756; 五年影响因子:2.752 )
ISSN:
年卷期:
页码:
收录情况: SCI
摘要: 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.
分类号: Q5
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