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Shape evolution with temperature of a thermotolerant protein ( PeaT 1) in solution detected by small angle X‐ray scattering
Author(s) -
Xing Xueqing,
Liu Quan,
Wang Wei,
Zhang Kunhao,
Li Tang,
Cai Quan,
Mo Guang,
Cheng Weidong,
Wang Dehong,
Gong Yu,
Chen Zhongjun,
Qiu Dewen,
Wu Zhonghua
Publication year - 2013
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.24162
Subject(s) - small angle x ray scattering , scattering , peat , crystallography , chemistry , protein structure , synchrotron radiation , valence (chemistry) , chemical physics , physics , optics , biology , biochemistry , organic chemistry , ecology
The protein elicitor from Alternaria tenuissima ( PeaT 1) presented excellent thermotolerance and potential application in agriculture as a pesticide. Previous synchrotron radiation circular dichroism study demonstrated that the secondary structures in PeaT 1 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 PeaT 1 protein with temperature in this article. Ab initio structure restorations based on the SAXS data revealed that PeaT 1 protein has a prolate shape with a P 2 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. PeaT 1 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.