Open Access
Proceedings of the Sixth National Conference on Application of X-Ray, Synchrotron Radiation, Neutrons and Electrons for Material Characterization (Shubnikov Institute of Crystallography RAS, Moscow, 2007)

Journal of Surface Investigation. X-ray, Synchrotron and Neutron Techniques

, 2:894

Comparative analysis of sensory rhodopsin II structures in complex with a transducer and without it

Authors

  • A. B. Reshetnyak
    • Institute of Structural Biology
    • Physico-Technical InstituteCenter of Biophysics and Physico-Chemistry of Permolecular Structures
  • V. I. Borshchevskiy
    • Institute of Structural Biology
    • Physico-Technical InstituteCenter of Biophysics and Physico-Chemistry of Permolecular Structures
  • J. Klare
    • Max-Planck Institute of Molecular Physiology
  • E. S. Moiseeva
    • Institute of Structural Biology
    • Physico-Technical InstituteCenter of Biophysics and Physico-Chemistry of Permolecular Structures
  • M. Engelhardt
    • Max-Planck Institute of Molecular Physiology
  • G. Buldt
    • Institute for Neurobiology and Biophysics 2
  • V. I. Gordeliy
    • Institute of Structural Biology
    • Physico-Technical InstituteCenter of Biophysics and Physico-Chemistry of Permolecular Structures
    • Frank Laboratory of Neutron PhysicsJoint Institute for Nuclear Research
    • Institute for Neurobiology and Biophysics 2

DOI: 10.1134/S1027451008060128

Abstract

Sensory rhodopsin II (NpSRII) is a heptahelical transmembrane protein containing the retinal chromophore. In complex with another membrane protein, i.e., NpHtrII transducer, NpSRII transmits a signal into a cell, initiating negative phototaxis of Natronobacterium pharaonis. In the absence of a transducer, rhodopsin II can work as a proton pump similar to bacteriorhodopsin. The main objective of this study is to comparatively analyze receptor structures in complex with the transducer and without it to understand the mechanism of the protein switching function. Diffraction data for sensory rhodopsin II crystals grown in the lipidic cubic phase were obtained at the synchrotron x-ray source. In this paper, we present a new NpSRII structure with a resolution of 2.1 Å and the results of a comparative analysis of the obtained NpSRII structure with our previously published data on the NpSRII/NpHtrII complex structure and with two NpSRII structures without a transducer, previously published in the literature.

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© MAIK Nauka 2008