Intrinsic disorder and metal binding in UreG proteins from Archae hyperthermophiles: GTPase enzymes involved in the activation of Ni(II) dependent urease

@article{Miraula2015IntrinsicDA,
  title={Intrinsic disorder and metal binding in UreG proteins from Archae hyperthermophiles: GTPase enzymes involved in the activation of Ni(II) dependent urease},
  author={Manfredi Miraula and S. Ciurli and B. Zambelli},
  journal={JBIC Journal of Biological Inorganic Chemistry},
  year={2015},
  volume={20},
  pages={739-755}
}
  • Manfredi Miraula, S. Ciurli, B. Zambelli
  • Published 2015
  • Chemistry, Medicine
  • JBIC Journal of Biological Inorganic Chemistry
  • Urease is a Ni(II) enzyme present in every domain of life, in charge for nitrogen recycling through urea hydrolysis. Its activity requires the presence of two Ni(II) ions in the active site. These are delivered by the concerted action of four accessory proteins, named UreD, UreF, UreG and UreE. This process requires protein flexibility at different levels and some disorder-to-order transition events that coordinate the mechanism of protein–protein interaction. In particular, UreG, the GTPase in… CONTINUE READING
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