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Structural and mechanistic insight from high resolution structures of archaeal rhodopsins
Author(s) -
Landau Ehud M,
Pebay-Peyroula Eva,
Neutze Richard
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01082-2
Subject(s) - bacteriorhodopsin , rhodopsin , halorhodopsin , halobacterium salinarum , biophysics , archaea , biology , functional divergence , energy landscape , protein structure , chemistry , biochemistry , retinal , gene , membrane , genome , gene family
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.