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Issue 21, 2015
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Specificity of the Zn2+, Cd2+ and Ni2+ ion binding sites in the loop domain of the HypA protein

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Abstract

The zinc binding loop domain of the HypA protein of Helicobacter pylori consists of two CXXC motifs with flanking His residues. These motifs bind metal ions, and thus they are crucial for the functioning of the whole protein. The N-terminal site, where His is separated from CXXC by Ser residue is more effective in binding Zn2+ and Ni2+ ions than the C-terminal site, in which His is adjacent to the CXXC motif. Studies on various modifications of the peptide sequence within the Ac-ELECKDCSHVFKPNALDYGVCEKCHS-NH2 loop show the role of the residues in the linker between the CXXC motifs and the effect of the length of the linker on the stability of the complexes it forms with Zn2+, Cd2+ and Ni2+ ions. The proline residue in the linker between the two CXXC binding sites plays a distinct role in the metal ion binding ability of the loop, lowering the efficacy of the metal ion coordination. The deletion of the aliphatic residues from the linker between the CXXC motifs remarkably improves the binding efficacy of the loop.

Graphical abstract: Specificity of the Zn2+, Cd2+ and Ni2+ ion binding sites in the loop domain of the HypA protein

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Supplementary files

Article information


Submitted
13 Mar 2015
Accepted
20 Apr 2015
First published
22 Apr 2015

Dalton Trans., 2015,44, 9887-9900
Article type
Paper
Author version available

Specificity of the Zn2+, Cd2+ and Ni2+ ion binding sites in the loop domain of the HypA protein

P. Kolkowska, K. Krzywoszynska, S. Potocki, P. R. Chetana, M. Spodzieja, S. Rodziewicz-Motowidlo and H. Kozlowski, Dalton Trans., 2015, 44, 9887
DOI: 10.1039/C5DT01005E

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