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 ,
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