NMR structure of the histidine kinase domain of the E.coli osmosensor EnvZ
Article Abstract:
Bacteria have to sense external conditions so that they can adjust their motility, physiology and shape. The histidine-aspartate phosphorelay signal-transduction system adapts to changes in both prokaryotes and lower eukaryotes. EnvZ, the Escherichia coli osmosensor, has histidine kinase activity in its cytoplasmic region, which contains domain A and the conserved histidine residue (H243). The solution structure of the catalytic core of EnvZ, domain B, with a novel protein kinase structure, is presented.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1998
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Molecular mechanisms of calcium-myristoyl switches
Article Abstract:
Biochemical research using nuclear magnetic resonance and X-ray crystallography demonstrates that the myristoyl group of the protein recoverin unclamps from EF hands in the presence of Ca2+. The myristoyl group interacts with the recoverin lipid bilayer membrane. Evidence suggests that the calcium-myristoyl switches manage calcium-sensitive physiological activities in the cells of eukaryotic and viruses.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
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Sequestration of the membrane-targeting myristoyl group of recoverin in the calcium-free state
Article Abstract:
Heteronuclear multidimensional nuclear magnetic resonance spectroscopy can be used to obtain the solution structure of calcium ion-free, myristoylated recombinant recoverin. This solution structure could provide insights into myristoyl switch states through the myristoyl group's sequestration within recoverin. Recoverin is involved in background light adaptation and the visual excitation recovery phase.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1995
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