Imaging bacteriorhodopsin-like molecules of claret-membranes from Tibet halobacteria xz515 by atomic force microscope

作     者：TANG Lin SUN Qing’an LI Qingguo HUANG Yibo WEI Qingqing ZHANG Yi HU Jun ZHANG Zhihong LI Minqian YANG Fujia 

作者机构：Laboratory of Detection and Manipulation of Single MoleculeShanghai Institute of Nuclear ResearchChinese Academy of SciencesShanghai 201800China Liren LaboratoryDepartment of Physiology and BiophysicsSchool of Life SciencesFudan UniversityShanghai 200433China Laboratory of NeurobiologyShanghai Institute of PhysiologyChinese Academy of SciencesShanghai 200031China Moden Institute of PhysicsFudan UniversityShanghai 200433China Center for Bio-X Science StudyShanghai Jiao Tong UniversityShanghai 200030China 

出 版 物：《Chinese Science Bulletin》 (CHINESE SCIENCE BULLETIN)

年 卷 期：2001年第46卷第22期

页      面：1897-1900页

核心收录：

学科分类：071011[理学-生物物理学] 0710[理学-生物学] 07[理学] 

基　　金：This work was supported by the National Natural Science Foundation of China (Grant Nos. 19890385, 39730150 and 19725415) the key programs of the Chinese Academy of Sciences (Grant Nos.KJ951-A1-603, KJ951-A1-409, KJ952-J1-469 and STZ-00-07) 

主　　题：atomic force microscope archaerhodopsin bacteri- orhodopsin hexagonal lattice halobacteria. 

摘      要：Halobacteria *** 515 was isolated from a salt lake in Tibet. Although proton release-and-uptake across claret membrane is in reverse order compared to bacteri-orhodopsin in purple membrane from Halobacterium Sali-narum, and its efficiency of proton pump is much lower, AFM image shows that the molecules are still arranged in a two-dimensional hexagonal lattice of trimers. Primary structure of C- to G-helix of the archaerhodopsin shows that it has only 56% homology with bacteriorhodopsin. But the interactive amino acid residues at the interface between B-and D-helixes are conserved. These amino acid residues are believed to play a significant role in the stability of protein oligomers.