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Inne
The -Cys-Cys-motif in Helicobacter pylori's Hpn and HspA proteins is an essential anchoring site for metal ions.
Autorzy
Rok wydania
2011
Czasopismo
Numer woluminu
40
Strony
5604-5610
DOI
10.1039/c1dt10187k
Kolekcja
Język
Angielski
Typ publikacji
Artykuł
The Hpn and HspA proteins fromH. pyloriare significant for nickel homeostasis and protect the cellsfrom higher concentrations of external metal ions. Both proteins have a unique histidine- andcysteine-rich domain at the C terminus.The interactions of Ni2+,Bi3+,Zn2+and Cd2+ions with C-terminal Ac–CCSTSDSHHQ–NH2andAc–EEGCCHGHHE–NH2fragments from Hpn and the Ac–GSCCHTGNHD–NH2sequence fromHspA were studied by potentiometry, mass spectrometry, circular dichroism and UV-Vis spectroscopy.Ac–CC–NH2was used as a reference peptide. The studies have shown that nickel ions form planarcomplexes with a{2S-,N-}binding mode. The thiol sulfurs of the –Cys–Cys– motif are also theanchoring sites for Bi3+,Zn2+and Cd2+ions. The studied protein fragments have the highest affinity forBi3+ions. The thermodynamic stability of Ni2+is much higher then that of Zn2+
Adres publiczny
http://dx.doi.org/10.1039/c1dt10187k