Shape evolution with temperature of a thermotolerant protein (PeaT1) in solution detected by small angle X-ray scattering
Xing XQ(邢雪青); Xing, XQ; Wang W(王维); Liu, Q; Wang, W; Zhang, KH; Li, T; Cai, Q; Mo, G; Cheng, WD; Wang, DH; Gong, Y; Chen, ZJ; Qiu, DW; Wu, ZH; Zhang KH(张坤浩);  Cai Q(蔡泉);  Mo G(默广);  Cheng WD(程伟东);  Wang DH(王德红);  Gong Y(宫宇);  Chen ZJ(陈中军);  Wu ZH(吴忠华)
刊名PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
2013
卷号81期号:1页码:53-62
关键词domain structure restoration structure prediction SRCD SAXS PeaT1
学科分类Biochemistry & Molecular Biology; Biophysics
DOI10.1002/prot.24162
英文摘要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 degrees C), to jug-like (55 degrees C), then to oval (85 degrees 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. (c) 2012 Wiley Periodicals, Inc.
收录类别SCI
WOS记录号WOS:000312551700004
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被引频次:2[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://ir.ihep.ac.cn/handle/311005/223803
专题中国科学院高能物理研究所_多学科研究中心_期刊论文
中国科学院高能物理研究所_多学科研究中心
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Xing XQ,Xing, XQ,Wang W,et al. Shape evolution with temperature of a thermotolerant protein (PeaT1) in solution detected by small angle X-ray scattering[J]. PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS,2013,81(1):53-62.
APA 邢雪青.,Xing, XQ.,王维.,Liu, Q.,Wang, W.,...&张坤浩;蔡泉;默广;程伟东;王德红;宫宇;陈中军;吴忠华.(2013).Shape evolution with temperature of a thermotolerant protein (PeaT1) in solution detected by small angle X-ray scattering.PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS,81(1),53-62.
MLA 邢雪青,et al."Shape evolution with temperature of a thermotolerant protein (PeaT1) in solution detected by small angle X-ray scattering".PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS 81.1(2013):53-62.
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