Novel insights into the metal binding ability of ZinT periplasmic protein from <i>Escherichia coli</i> and <i>Salmonella enterica</i>
Denise Bellotti, Magdalena Rowińska‐Żyrek, Maurizio Remelli
Abstract
from the ZinT protein expressed by Salmonella enterica sv. Typhimurium (SeZinT). The investigated peptides are able to form stable mono-nuclear complexes where the histidine residues represent the principal metal anchoring sites. The ZnuA (a periplasmic component of the ZnuABC transporter) metal binding site exhibits higher affinity for Zn(ii) than ZinT, suggesting that the interaction of the two proteins through the formation of a binary complex may involve the metal transfer from ZinT to ZnuA. In contrast, this would not occur in Cu(ii), since the ZinT complexes are more stable. Furthermore, at acidic pH, where the antimicrobial peptide calcitermin is biologically active, it also binds the metal ions with higher affinity than ZinT, representing a possible efficient competitor and antagonist of ZinT in the host human organism.