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Pneumococcal histidine triads – involved not only in Zn2+, but also Ni2+ binding?

Abstract

Polyhistidine triad proteins, which participate in Zn2+ uptake in Streptococcus pneumoniae, contain multiple copies of the HxxHxH (histidine triad motif) sequence. We focus on three such motifs from one of the most common and well-conserved polyhistidine triad proteins, PhtA, in order to understand their bioinorganic chemistry; particular focus is given to (i) understanding which of the PhtA triads binds Zn2+ with the highest affinity (and why?) and (ii) explaining if Ni2+ (also crucial for bacterial survival and virulence) could potentially outcompete Zn2+ from its native binding site. There is no significant difference in the stability of zinc(II) complexes with the three studied protein fragments, but one of the nickel(II)-polyhistidine triad is remarkably stable; we explain why and hypothesize about the biological importance of this finding.

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Publication details

The article was accepted on 09 Oct 2018 and first published on 09 Oct 2018


Article type: Paper
DOI: 10.1039/C8MT00275D
Citation: Metallomics, 2018, Accepted Manuscript
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    Pneumococcal histidine triads – involved not only in Zn2+, but also Ni2+ binding?

    A. Miller, D. Loboda, S. Potocki, H. Czapor-Irzabek, H. Kozlowski and M. Rowinska-Zyrek, Metallomics, 2018, Accepted Manuscript , DOI: 10.1039/C8MT00275D

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