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Crystal structures of the PsbS protein essential for photoprotection in plants,Nature Structural & Molecular Biology, Published online 10 August 2015

发布时间:2015年08月11日

Nature Structural & Molecular Biology, Published online 10 August 2015, DOI: doi:10.1038/nsmb.3068

Crystal structures of the PsbS protein essential for photoprotection in plants

Minrui Fan,1, 2, Mei Li,1, Zhenfeng Liu,1, Peng Cao,1, Xiaowei Pan,1, Hongmei Zhang,1, Xuelin Zhao,1, Jiping Zhang1, & Wenrui Chang1,

Abstract

The photosystem II protein PsbS has an essential role in qE-type nonphotochemical quenching, which protects plants from photodamage under excess light conditions. qE is initiated by activation of PsbS by low pH, but the mechanism of PsbS action remains elusive. Here we report the low-pH crystal structures of PsbS from spinach in its free form and in complex with the qE inhibitor N,N′-dicyclohexylcarbodiimide (DCCD), revealing that PsbS adopts a unique folding pattern, and, unlike other members of the light-harvesting-complex superfamily, it is a noncanonical pigment-binding protein. Structural and biochemical evidence shows that both active and inactive PsbS form homodimers in the thylakoid membranes, and DCCD binding disrupts the lumenal intermolecular hydrogen bonds of the active PsbS dimer. Activation of PsbS by low pH during qE may involve a conformational change associated with altered lumenal intermolecular interactions of the PsbS dimer.

文章链接:http://www.nature.com/nsmb/journal/vaop/ncurrent/full/nsmb.3068.html

相关报道:http://www.ibp.cas.cn/kyjz/zxdt/201508/t20150811_4409338.html

 

 

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