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Papers In Press, published online ahead of print October 7, 2003
Department of Chemistry and Bioscience, Chalmers University of Technology, Gothenburg S-40530
Corresponding Author: neutze{at}molbiotech.chalmers.se
X-ray and electron diffraction studies of specific reaction intermediates, or reaction intermediate analogues, have produced a consistent picture of the structural mechanism of light-driven proton pumping by bacteriorhodopsin. Of central importance within this picture is the structure of the L-intermediate, which follows the retinal all trans to 13-cis photoisomerization step of the K-intermediate, and sets the stage for the primary proton transfer event from the positively charged Schiff base to the negatively charged Asp85. Here we report the structural changes in bacteriorhodopsin following red-light illumination at 150 K. Single crystal microspectrophotometry shows that only the L-intermediate is populated in 3D crystals under these conditions. The experimental difference Fourier electron density map and refined crystallographic structure are consistent with those previously presented. Based on the refined crystallographic structures, molecular dynamics simulations are used to examine the influence of the protein’s conformational change associated with the K-to-L transition on retinal dynamics. Implications regarding the structural mechanism for proton pumping by bacteriorhodopsin are discussed.
J. Biol. Chem, 10.1074/jbc.M300709200
Submitted on January 22, 2003
Revised on October 7, 2003
Accepted on October 7, 2003
Deformation of helix C in the low-temperature L-intermediate of bacteriorhodopsin
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