Molecular modeling of the HAMP domain of sensory rhodopsin II transducer from Natronomonas pharaonis
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Molecular modeling of the HAMP domain of sensory rhodopsin II transducer from Natronomonas pharaonis
The halobacterial transducer of sensory rhodopsin II (HtrII) is a photosignal transducer associated with phototaxis in extreme halophiles. The HAMP domain, a linker domain in HtrII, is considered to play an important role in transferring the signal from the membrane to the cytoplasmic region, although its structure in the complex remains undetermined. To establish the structural basis for under...
متن کاملFlexibility of the Cytoplasmic Domain of the Phototaxis Transducer II from Natronomonas pharaonis
Chemo- and phototaxis systems in bacteria and archaea serve as models for more complex signal transduction mechanisms in higher eukaryotes. Previous studies of the cytoplasmic fragment of the phototaxis transducer (pHtrII-cyt) from the halophilic archaeon Natronomonas pharaonis showed that it takes the shape of a monomeric or dimeric rod under low or high salt conditions, respectively. CD spect...
متن کاملTwo Distinct States of the HAMP Domain from Sensory Rhodopsin Transducer Observed in Unbiased Molecular Dynamics Simulations
HAMP domain is a ubiquitous module of bacterial and archaeal two-component signaling systems. Considerable progress has been made recently in studies of its structure and conformational changes. However, the mechanism of signal transduction through the HAMP domain is not clear. It remains a question whether all the HAMPs have the same mechanism of action and what are the differences between the...
متن کاملHAMP domain signal relay mechanism in a sensory rhodopsin-transducer complex.
The phototaxis receptor complex composed of sensory rhodopsin II (SRII) and the transducer subunit HtrII mediates photorepellent responses in haloarchaea. Light-activated SRII transmits a signal through two HAMP switch domains (HAMP1 and HAMP2) in HtrII that bridge the photoreceptive membrane domain of the complex and the cytoplasmic output kinase-modulating domain. HAMP domains, widespread sig...
متن کاملRole of Asp193 in chromophore-protein interaction of pharaonis phoborhodopsin (sensory rhodopsin II).
Pharaonis phoborhodopsin (ppR; also pharaonis sensory rhodopsin II, psRII) is a receptor of the negative phototaxis of Natronobacterium pharaonis. By spectroscopic titration of D193N and D193E mutants, the pK(a) of the Schiff base was evaluated. Asp193 corresponds to Glu204 of bacteriorhodopsin (bR). The pK(a) of the Schiff base (SBH(+)) of D193N was approximately 10.1-10.0 (at XH(+)) and appro...
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ژورنال
عنوان ژورنال: BIOPHYSICS
سال: 2010
ISSN: 1349-2942
DOI: 10.2142/biophysics.6.27