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
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