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Biophysical Journal 85:451-458 (2003)
© 2003 The Biophysical Society

Crystal Structure of the Bromide-Bound D85S Mutant of Bacteriorhodopsin: Principles of Ion Pumping

Marc T. Facciotti * {dagger}, Vincent S. Cheung {ddagger}, Doris Nguyen §, Shahab Rouhani {dagger} and Robert M. Glaeser * {dagger} {ddagger}

* Graduate Group in Biophysics, University of California, Berkeley, California 94720; {dagger} Life Sciences Division, Donner Laboratory, Lawrence Berkeley National Laboratory, Berkeley, California 94720; {ddagger} Department of Molecular and Cell Biology, Stanley/Donner ASU, University of California, Berkeley, California 94720-3206; and § Department of Bioengineering, University of California, Berkeley, California 94720

Correspondence: Address reprint requests to Robert M. Glaeser, E-mail: rmglaeser{at}lbl.gov.

We report the crystal structure of a bromide-bound form of the D85S mutant of bacteriorhodopsin, bR(D85S), a protein that uses light energy rather than ATP to pump halide ions across the cell membrane. Comparison of the structure of the halide-bound and halide-free states reveals that both displacements of individual side-chain positions and concerted helical movements occur on the extracellular side of the protein. Analysis of these structural changes reveals how this ion pump first facilitates ion uptake deep within the cell membrane and then prevents the backward escape of ions later in the pumping cycle. Together with the information provided by structures of intermediate states in the bacteriorhodopsin photocycle, this study also suggests the overall design principles that are necessary for ion pumping.




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