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|Title:||The zinc-binding fragment of HypA from Helicobacter pylori: a tempting site also for nickel ions||Authors:||Rowinska Zyrek, Magdalena
|Keywords:||Amino Acid Motifs; Bacterial Proteins; Carrier Proteins; Circular Dichroism; Coordination Complexes; Helicobacter pylori; Ions; Molecular Sequence Data; Nickel; Protein Binding; Sequence Alignment; Thermodynamics; Zinc||Issue Date:||2013||Project:||None||Journal:||DALTON TRANSACTIONS||Abstract:||
HypA, a nickel accessory protein from H. pylori, binds a zinc ion in it's structural site, a loop with two conserved CXXC motifs (Ac-ELECKDCSHVFKPNALDYGVCEKCHS-NH(2)). There are at least three hypotheses on the binding mode of this ion. In this paper, we try to understand how Zn(2+) binds to this fragment and why Ni(2+), a metal with quite a high affinity towards thiolic sites, doesn't compete with zinc in the binding to this motif. Potentiometric titrations, mass spectrometry, NMR, UV-Vis and CD spectroscopy help us to compare the coordination modes in both metal complexes and discuss their thermodynamic stabilities.
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