常文瑞院士----中国科学院生物物理研究所

简历 & 研究组工作摘要：
        1990年至今中国科学院生物物理研究所研究员，生物大分子国家重点实验室学术委员
        中国科学院院士
        作为课题负责人主持并完成了一系列蛋白质三维结构测定，多次获得国家级和科学院奖励

        研究重点集中在光合作用系统中的膜蛋白复合物的结构与功能，在解析三维结构的基础上，结合生化和光谱学手段，开展植物光能传递以及光保护的机理研究。主要工作集中在不同种属高等植物（光系统II）PSII中光合作用相关膜蛋白及复合物的结晶和三维结构研究。
        解析了黄瓜LHC-II的2.66 欧直媛实木褰峁梗⑾至薒HCII分子中两个Lutein分子的构象差异, 提出这种构象改变可能与光淬灭位点的形成有关；并且发现不同存放期的LHCII晶体的晶胞参数和光谱特征有所改变，推测这种变化可能与其分子构象变化有关，并将可能为研究其光能传递和光保护提供新的信息, 部分研究结果已发表于BBRC，后续研究工作正在进展之中。
        同时开展了与人类健康和环境相关的重要功能蛋白的三维结构与功能研究,成功测定了马来酰丙酮酸异构酶以及该酶一种突变体的高分辨率晶体结构，这是第一个MSH依赖性酶的晶体结构，研究结果发表于J. Biol. Chem.。解析了人源S100A13蛋白的晶体结构，研究结果发表于BBRC。另外分别测定了蚯蚓纤溶酶三种组分：EFE-b、EFE-c、EFE-g和牛胰蛋白酶抑制剂aprotinin的复合物的高分辨率晶体结构，结果正在总结之中。

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Biography & Introduction

1990---- Professor of Structural Biology in Institute of Biophysics CAS.
Member of Chinese Academy of Sciences
As a group leader, have completed a series of 3D-structure determination of many proteins. Won several National and CAS's awards.

We mainly focus on research of the relationship between 3-D structure and function of photosynthesis membrane proteins based on X-ray crystallography. We are concentrated on the structure determination of light harvesting proteins and reaction center complexes from different plants trying to understand the basic mechanism of light harvesting and photo protection. The research interest is crystallization and structural study of higher plant photosystems, particularly photosystem II.

We have solved LHC-II crystal structure from cucumber at 2.66 angstrom resolution. It was found that two lutein molecules have different conformations. We proposed that the conformational change might relate to formation of non-photochemical quenching site based on the structure analysis. We also discovered that the dehydration of the LHCII crystals resulted in a notable shrinkage of the crystal unit cell dimensions which was accompanied by a red-shift of the fluorescence emission spectra of the crystals. These phenomena suggest the changes in the crystal packing during dehydration might be the cause of internal conformational changes within LHCII. Part of the results was published in BBRC.

Besides, we are also interested in the structure determination of some important proteins related to human health and environment. Recently, we have solved high resolution structures of native and a mutant of MPI, which is the first example of MSH-dependent enzyme. The results was summarized and published in JBC. We also solved crystal structure of human S100A13, the result was published in BBRC. In addition, three structures of EFE components complexed with inhibitor were also solved, the results were in summarization.

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Wang R, Yin YJ, Wang F, Li M, Feng J, Zhang HM, Zhang JP, Liu SJ, Chang WR. Crystal structures and site-directed mutagenesis of a mycothiol-dependent enzyme reveal a novel folding and molecular basis for mycothiol-mediated maleylpyruvate isomerization. J BIOL CHEM. 2007, 282(22):16288-294.

Li M, Zhang PF, Pan XW, Chang WR. Crystal structure study on human S100A13 at 2.0 angstrom resolution. BIOCHEM BIOPHYS RES COMMUN. 2007,356(3):616-21.

Yan H, Zhang P, Wang C, Liu Z, Chang WR. Two lutein molecules in LHCII have different conformations and functions: Insights into the molecular mechanism of thermal dissipation in plants. BIOCHEM BIOPHYS RES COMMUN. 2007 ,355(2):457-63.

Zhenfeng Liu， Hanchi Yan， Kebin Wang， Tingyun Kuang， Jiping Zhang， Lulu Gui， Xiaomin An & Wenrui Chang. Crystal structure of spinach major light-harvesting complex at 2.72 angstrom esolution. Nature 428, 287-292 (2004).

Hai-Tao Li, Chao Wang, Tschining Chang, Wen-Chang Chang, Ming-yih Liu, Jean Le Gall, Lu-Lu Gui, Ji-Ping Zhang, Xiao-Min An, Wen-Rui Chang. pH-profile crystal structure studies of C-terminal despentapeptide nitrite reductase from Achromobacter cycloclastes. BIOCHEM BIOPH RES CO 316, 107-113 (2004).

Sheng-Quan Liu, Tschining Chang, Ming-Yih Liu, Jean LeGall, Wen-Chang Chang, Ji-Ping Zhang, Dong-Cai Liang, and Wen-Rui Chang . Crystal structure of a NO-forming nitrite reductase mutant: an analog of a transition state in enzymatic reaction. BIOCHEM BIOPH RES CO 302, 568 – 574 (2003).

Mei Li、Ming-Yih Liu1、Jean Le Gall1、LU-Lu Gui、Jun Liao、Tao Jiang、Ji-Ping Zhang、Dong-cai Liang、Wen-rui Chang. Crystal structure studies on rubrerythrin: enzymatic activity in relation to the zinc movement. J BIOL INORG CHEM 8, 149-155 (2003).

Yong Tang, Dongcai Liang, Jiang Tao, Jiping Zhang, Lulu Gui, Wenrui Chang. Crystal structure of earthworm fibrinolytic enzyme component A: Revealing the structural determinanants of its dual fibrinolytic activity. J MOL BIOL 321, 57-68 (2002).