报告题目：Cryo-EM structure of the reaction center light harvesting complex 1 from photosynthetic  

bacterium Blastochloris viridis at 2.9 Å resolution

报告人： Dr. Pu Qian（钱朴）

     英国谢菲尔德大学(The University of Sheffield)，分子生物学与生物技术系

报告时间：2018年3月27日（周二）下午14:00-15:00

报告地点：下沙校区1号实验楼406室

Abstract

The reaction centre light-harvesting 1 (RC-LH1) complex is the core functional component of bacterial photosynthesis. A 2.9 Å resolution cryo-EM structure of the bacteriochlorophyll b-based RC-LH1 from Blastochloris viridis reveals the structural basis for absorption of infrared light, and the molecular mechanism of quinone migration across the LH1 complex. The novel triple ring LH1 complex comprises a circular array of 17 β-polypeptides sandwiched between 17 α- and 16 γ-polypeptides. Tight packing of the γ-apoproteins between βs collectively interlocks and stabilizes the LH1 structure which, together with the short Mg-Mg distances of BChl b pairs, contributes to the large red-shift of bacteriochlorophyll b absorption. The ‘missing’ 17^th γ polypeptide creates a pore in the LH1 ring, and an adjacent binding pocket provides a folding template for a novel quinone, Q_P, which adopts a compact, export-ready conformation prior to passage through the pore and eventual diffusion to the cytochrome bc₁ complex.

个人简介：

Pu Qian is a Professor (part-time), School of Life Science, Suzhou University and Research associate of Department of Molecular Biology & Biotechnology, The University of Sheffield, UK. His main research work are High resolution structures of light harvesting core complexes from photosynthetic bacteria using cryo-EM. His expertise include protein purification, 2D/3D crystallizations, EM measurement, data processing and presentation. 2D electron crystallography, X-ray crystallography and cryo-EM single particle analysis have been employed for structure determination of membrane proteins. During the last decade, he published a series of papers on the structure determination of RC-LH1 core complexes from photosynthetic bacteria. Recently, a 2.9 Å resolution cryo-EM structure of the core complexes from Blastochloris viridiswild was accepted by Nature as an article. This structure revealed a new architecture of the RC-LH1 core complex from photosynthetic bacteria, explained its large red-shift absorption of bacteriochlorophyll b in the complex and mechanism of quinone / quinol migration in the photosynthetic membrane.

联系人：辛越勇 15306529702

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