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.
Copyright © 2013 Elsevier B.V. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Archaeal Proteins / chemistry*
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Archaeal Proteins / genetics
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Archaeal Proteins / physiology
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Archaeal Proteins / radiation effects
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Carotenoids / chemistry*
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Carotenoids / genetics
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Carotenoids / radiation effects
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Crystallography, X-Ray
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Halobacteriaceae / chemistry
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Halorhodopsins / chemistry*
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Hydrogen Bonding
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Intracellular Signaling Peptides and Proteins / chemistry*
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Intracellular Signaling Peptides and Proteins / genetics
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Light
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Models, Molecular
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Multiprotein Complexes / chemistry
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Multiprotein Complexes / radiation effects
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Rhodopsins, Microbial / chemistry*
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Rhodopsins, Microbial / genetics
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Sensory Rhodopsins / chemistry*
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Signal Transduction
Substances
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Archaeal Proteins
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Halorhodopsins
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HtrII protein, Natronobacterium pharaonis
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Intracellular Signaling Peptides and Proteins
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Multiprotein Complexes
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Rhodopsins, Microbial
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Sensory Rhodopsins
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phototaxis receptor sensory rhodopsin II, Natronobacterium pharaonis
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Carotenoids