Structural and mechanistic insight from high resolution structures of archaeal rhodopsins

FEBS Letters

Neutze, Richard¹  Pebay-Peyroula, Eva³  Landau, Ehud M² 

[1] Department of Chemistry and Bioscience, Chalmers University of Technology, Box 462, S-40530 Gothenburg, Sweden;Membrane Protein Laboratory, Sealy Center for Structural Biology, and Department of Physiology and Biophysics, The University of Texas Medical Branch, 301 University Boulevard, Galveston, TX 77555-0437, USA;Institut de Biologie Structurale, UMR5075, CEA-CNRS-Université Joseph Fourier, 41 rue Jules Horowitz, F-38027 Grenoble Cedex 1, France

关键词: Archaeal rhodopsin;    Lipidic cubic phase;    Membrane protein;    Structural dynamics;    X-ray crystallography;   

DOI  :  10.1016/S0014-5793(03)01082-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Lipidic cubic phase-grown crystals yielded high resolution structures of a number of archaeal retinal proteins, the molecular mechanisms of which are being revealed as structures of photocycle intermediates become available. The structural basis for bacteriorhodopsin's mechanism of proton pumping is discussed, revealing a well-synchronized sequence of molecular events. Comparison with the high resolution structures of the halide pump halorhodopsin, as well as with the receptor sensory rhodopsin II, illustrates how small and localized structural changes result in functional divergence. Fundamental principles of energy transduction and sensory reception in the archaeal rhodopsins, which may have relevance to other systems, are discussed.

【 授权许可】

Unknown