Bacteriorhodopsin is a light-driven proton pump that has several well-characterized intermediates in its photocycle. The general aim of this proposal is to define the mechanism of proton transport in bacteriorhodopsin by mapping the conformational changes during the photocycle in atomic detail.
The specific aims are 1) to determine the high resolution structure of light-adapted (ground state) bacteriorhodopsin, 2) determine the structure of the M intermediate by solving the structure of D96N bacteriorhodopsin 3) determine the crystal structure of the K intermediate, 4) solve the crystal structure of the L intermediate and 5) solve the structure of a chloride pump, either halorhodopsin, or D85S bacteriorhodopsin, which functions as a chloride pump.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM059970-03
Application #
6387004
Study Section
Biophysical Chemistry Study Section (BBCB)
Program Officer
Lewis, Catherine D
Project Start
1999-09-01
Project End
2003-08-31
Budget Start
2001-09-01
Budget End
2002-08-31
Support Year
3
Fiscal Year
2001
Total Cost
$215,251
Indirect Cost
Name
University of California Irvine
Department
Biochemistry
Type
Schools of Arts and Sciences
DUNS #
161202122
City
Irvine
State
CA
Country
United States
Zip Code
92697
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Vogeley, Lutz; Sineshchekov, Oleg A; Trivedi, Vishwa D et al. (2004) Anabaena sensory rhodopsin: a photochromic color sensor at 2.0 A. Science 306:1390-3
Cartailler, Jean-Philippe; Luecke, Hartmut (2004) Structural and functional characterization of pi bulges and other short intrahelical deformations. Structure 12:133-44
Luecke, Hartmut; Lanyi, Janos K (2003) Structural clues to the mechanism of ion pumping in bacteriorhodopsin. Adv Protein Chem 63:111-30
Luecke, H; Schobert, B; Lanyi, J K et al. (2001) Crystal structure of sensory rhodopsin II at 2.4 angstroms: insights into color tuning and transducer interaction. Science 293:1499-503
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Spassov, V Z; Luecke, H; Gerwert, K et al. (2001) pK(a) Calculations suggest storage of an excess proton in a hydrogen-bonded water network in bacteriorhodopsin. J Mol Biol 312:203-19
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