منابع مشابه
Mutational analyses of HAMP helices suggest a dynamic bundle model of input-output signalling in chemoreceptors.
To test the gearbox model of HAMP signalling in the Escherichia coli serine receptor, Tsr, we generated a series of amino acid replacements at each residue of the AS1 and AS2 helices. The residues most critical for Tsr function defined hydrophobic packing faces consistent with a four-helix bundle. Suppression patterns of helix lesions conformed to the predicted packing layers in the bundle. Alt...
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متن کاملMutational analysis of a conserved signal-transducing element: the HAMP linker of the Escherichia coli nitrate sensor NarX.
The HAMP linker, a predicted structural element observed in sensor proteins from all domains of life, is proposed to transmit signals between extracellular sensory input domains and cytoplasmic output domains. HAMP (histidine kinase, adenylyl cyclase, methyl-accepting chemotaxis protein, and phosphatase) linkers are located just inside the cytoplasmic membrane and are projected to form two shor...
متن کاملMutational analysis of the connector segment in the HAMP domain of Tsr, the Escherichia coli serine chemoreceptor.
HAMP domains are approximately 50-residue motifs, found in many bacterial signaling proteins, that consist of two amphiphilic helices joined by a nonhelical connector segment. The HAMP domain of Tsr, the serine chemoreceptor of Escherichia coli, receives transmembrane input signals from the periplasmic serine binding domain and in turn modulates output signals from the Tsr kinase control domain...
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ژورنال
عنوان ژورنال: Molecular Microbiology
سال: 2009
ISSN: 0950-382X,1365-2958
DOI: 10.1111/j.1365-2958.2009.06818.x