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

First online:

Open Access This content is freely available online to anyone, anywhere at any time.

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

  • A. B. ReshetnyakAffiliated withInstitute of Structural BiologyPhysico-Technical Institute, Center of Biophysics and Physico-Chemistry of Permolecular Structures
  • , V. I. BorshchevskiyAffiliated withInstitute of Structural BiologyPhysico-Technical Institute, Center of Biophysics and Physico-Chemistry of Permolecular Structures
  • , J. KlareAffiliated withMax-Planck Institute of Molecular Physiology
  • , E. S. MoiseevaAffiliated withInstitute of Structural BiologyPhysico-Technical Institute, Center of Biophysics and Physico-Chemistry of Permolecular Structures
  • , M. EngelhardtAffiliated withMax-Planck Institute of Molecular Physiology
  • , G. BuldtAffiliated withInstitute for Neurobiology and Biophysics 2
  • , V. I. GordeliyAffiliated withInstitute of Structural BiologyPhysico-Technical Institute, Center of Biophysics and Physico-Chemistry of Permolecular StructuresFrank Laboratory of Neutron Physics, Joint Institute for Nuclear ResearchInstitute for Neurobiology and Biophysics 2 Email author 

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.