Structural and mechanistic insight from high resolution structures of archaeal rhodopsins.
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.
Landau
Ehud M
EM
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. emlandau@utmb.edu
Pebay-Peyroula
Eva
E
Neutze
Richard
R
D019843:Archaeal Proteins / Q000737:chemistry* / Q000378:metabolism*; D001665:Binding Sites; D008958:Models, Molecular; D015394:Molecular Structure; D018462:Photobiology; D011487:Protein Conformation; D012243:Rhodopsin / Q000737:chemistry* / Q000378:metabolism*
D019843:Archaeal Proteins; D012243:Rhodopsin