Electron crystallographic analysis of two-dimensional crystals of sensory rhodopsin II: a 6.9 A projection structure

Journal of Molecular Biology
E R KunjiJ L Spudich

Abstract

Sensory rhodopsins, phototaxis receptors in Haloarchaea, were purified and reconstituted into halobacterial lipids to form photoactive two-dimensional crystals. Images of vitreous ice-embedded, flattened, tubular crystals of sensory rhodopsin II (SRII) of Natronobacterium pharaonis were recorded using a field emission gun electron cryo-microscope. Fourier components for the SRII structure were determined either from the separated image transforms from single layers that formed each side of flattened tubes, or by a deconvolution procedure when two layers were stacked in register so that they generated a single crystal lattice by superposition. Most micrographs showed significant diffraction to 6.9 A after computer processing, and the results provide the first intermediate- resolution information obtained for an archaeal sensory rhodopsin. The projection structure of SRII indicates that the helix positions match the seven-helix arrangement of the archaeal transport rhodopsins rather than that of the eukaryotic visual pigments. The structural similarity of SRII to the transport rhodopsins supports models in which the transport and signalling mechanisms of archaeal rhodopsins derive from the same retinal-driven changes in protein c...Continue Reading

Citations

Sep 30, 2004·Biophysical Journal·Keiichi InoueMasahide Terazima
Apr 14, 2012·Journal of Fish Biology·T J LisneyN S Hart
Aug 2, 2003·The Journal of Biological Chemistry·Edmund R S Kunji, Marilyn Harding
Jun 25, 2003·The Journal of Biological Chemistry·Vladislav BergoKenneth J Rothschild
Nov 25, 2003·Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences·Yasuhiro Kashino
Jun 1, 2005·Journal of Molecular Biology·Andreas D SchenkAndreas Engel

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