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Published Online July 12, 2001 Science
DOI: 10.1126/science.1062977
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Reports
Submitted on May 30, 2001
Accepted on June 27, 2001
Crystal Structure of Sensory Rhodopsin II at 2.4 Å: Insights into Color Tuning and Transducer Interaction
Hartmut Luecke 1*,
Brigitte Schobert 2,
Janos K. Lanyi 2*,
Elena N. Spudich 3,
John L. Spudich 3*
1 Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697, USA; Department of Physiology and Biophysics, University of California, Irvine, CA 92697, USA.
2 Department of Physiology and Biophysics, University of California, Irvine, CA 92697, USA.
3 Department of Microbiology and Molecular Genetics and Structural Biology Center, University of Texas Medical School, Houston, TX 77030, USA.
* To whom correspondence should be addressed. E-mail: john.l.spudich{at}uth.tmc.edu.
We report an atomic resolution structure for a sensory member of the microbial rhodopsin family, the phototaxis receptor sensory rhodopsin II (NpSRII) that mediates blue-light avoidance by the haloarchaeon Natronobacterium pharaonis. The 2.4 Å structure reveals features responsible for the 70-80 nm blue-shift of its absorption maximum relative to those of haloarchaeal transport rhodopsins, and structural differences due to its sensory, as opposed to transport, function. Multiple factors appear to account for the spectral tuning difference with respect to bacteriorhodopsin: 1) repositioning of the guanidinium group of Arg72, a residue that interacts with the counterion to the retinylidene protonated Schiff base, 2) rearrangement of the protein near the retinal ring, and 3) changes in tilt and slant of the retinal polyene chain. Inspection of the surface topography reveals an exposed polar residue, Tyr199, not present in bacteriorhodopsin, in the middle of the membrane bilayer. We propose this residue interacts with the adjacent helices of the cognate NpSRII transducer NpHtrII.
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