• Title of article

    Ground state structure of D75N mutant of sensory rhodopsin II in complex with its cognate transducer

  • Author/Authors

    Ishchenko، نويسنده , , A. and Round، نويسنده , , E. and Borshchevskiy، نويسنده , , V. and Grudinin، نويسنده , , S. and Gushchin، نويسنده , , I. and Klare، نويسنده , , J.P. and Balandin، نويسنده , , T. and Remeeva، نويسنده , , A. and Engelhard، نويسنده , , M. and Büldt، نويسنده , , G. and Gordeliy، نويسنده , , V.، نويسنده ,

  • Issue Information
    روزنامه با شماره پیاپی سال 2013
  • Pages
    4
  • From page
    55
  • To page
    58
  • Abstract
    The complex of sensory rhodopsin II (NpSRII) with its cognate transducer (NpHtrII) mediates negative phototaxis in halobacteria Natronomonas pharaonis. Upon light activation NpSRII triggers, by means of NpHtrII, a signal transduction chain homologous to the two component system in eubacterial chemotaxis. Here we report on the crystal structure of the ground state of the mutant NpSRII-D75N/NpHtrII complex in the space group I212121. Mutations of this aspartic acid in light-driven proton pumps dramatically modify or/and inhibit protein functions. However, in vivo studies show that the similar D75N mutation retains functionality of the NpSRII/NpHtrII complex. The structure provides the molecular basis for the explanation of the unexpected observation that the wild and the mutant complexes display identical physiological response on light excitation.
  • Keywords
    X-ray crystallography , protein crystallization , Signal transduction , membrane protein , retinal protein
  • Journal title
    Journal of Photochemistry and Photobiology B:Biology
  • Serial Year
    2013
  • Journal title
    Journal of Photochemistry and Photobiology B:Biology
  • Record number

    1878404