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Pneumococcal histidine triads – involved not only in Zn2+, but also Ni2+ binding?
Autorzy
Rok wydania
2018
Czasopismo
Numer woluminu
10
Strony
1631-1637
DOI
10.1039/c8mt00275d
Kolekcja
Język
Angielski
Typ publikacji
Artykuł
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 whether Ni2+ (also crucial for bacterial survival and virulence) could potentially outcompete Zn2+ at 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 triads is remarkably stable; we explain why and hypothesize about the biological importance of this finding.
Adres publiczny
http://dx.doi.org/10.1039/c8mt00275d
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