Biochemical characterization of the tandem HAMP domain fromNatronomonas pharaonisas an intraprotein signal transducer
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چکیده
منابع مشابه
HAMP 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 کاملMolecular 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 کاملHAMP Domain Rotation and Tilting Movements Associated with Signal Transduction in the PhoQ Sensor Kinase
UNLABELLED HAMP domains are α-helical coiled coils that often transduce signals from extracytoplasmic sensing domains to cytoplasmic domains. Limited structural information has resulted in hypotheses that specific HAMP helix movement changes downstream enzymatic activity. These hypotheses were tested by mutagenesis and cysteine cross-linking analysis of the PhoQ histidine kinase, essential for ...
متن کاملThe HAMP Signal Relay Domain Adopts Multiple Conformational States through Collective Piston and Tilt Motions
The HAMP domain is a linker region in prokaryotic sensor proteins and relays input signals to the transmitter domain and vice versa. Functional as a dimer, the structure of HAMP shows a parallel coiled-coil motif comprising four helices. To date, it is unclear how HAMP can relay signals from one domain to another, although several models exist. In this work, we use molecular simulation to test ...
متن کاملSignal transducer gp130: biochemical characterization of the three membrane-proximal extracellular domains and evaluation of their oligomerization potential.
Glycoprotein 130 (gp130) is a type I transmembrane protein and serves as the common signal-transducing receptor subunit of the interleukin-6-type cytokines. Whereas the membrane-distal half of the gp130 extracellular part confers ligand binding and has been subject to intense investigation, the structural and functional features of its membrane-proximal half are poorly understood. On the basis ...
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ژورنال
عنوان ژورنال: FEBS Journal
سال: 2014
ISSN: 1742-464X
DOI: 10.1111/febs.12855