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High Resolution Structure of Bacteriorhodopsin Determined by Electron Crystallography
Author(s) -
Kimura Yoshiaki,
Vassylyev Dmitry G.,
Miyazawa Atsuo,
Kidera Akinori,
Matsushima Masaaki,
Mitsuoka Kaoru,
Murata Kazuyoshi,
Hirai Teruhisa,
Fujiyoshi Yoshinori
Publication year - 1997
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1997.tb03221.x
Subject(s) - bacteriorhodopsin , resolution (logic) , crystallography , chemistry , proton , halobacteriaceae , cytoplasm , electron crystallography , aspartic acid , protein structure , halobacterium , electron transfer , physics , membrane , halobacterium salinarum , amino acid , optics , electron diffraction , biochemistry , diffraction , quantum mechanics , artificial intelligence , computer science
— Bacteriorhodopsin pumps protons from the cytoplasm to the outside of halobacteria, Halobacterium salinarium , by using absorbed light energy. The newly observed density map at 3 Å resolution clarified nearly the entire structure; the resolution in the direction perpendicular to the membrane surface is 3.2 Å. The new structure clearly indicates the proton transfer pathway in bacteriorhodopsin. In particular, the location of key aspartic acid and glutamic acid residues in the derived structural model suggested funneling structures with different designs for input and output of protons on the cytoplasmic and extracellular sides, respectively, of the protein. This paper describes the major differences between the model based on the new observation and the former model obtained through crystallographic refinement by Grigorieff et al . ( J. Mol. Biol 259; 393‐421, 1996).