Specific Zn(II) binding site in the C-terminus of Aspf2, a zincophore from Aspergillus fumigatus

Metallomics. 2022 Jun 14:mfac042. doi: 10.1093/mtomcs/mfac042. Online ahead of print.


Aspergillus fumigatus, one of the most widespread opportunistic human fungal pathogens, adapts to zinc limitation by secreting a 310 amino acid Aspf2 zincophore, able to specifically bind Zn(II) and deliver it to a transmembrane zinc transporter, ZrfC. In this work, we focus on the thermodynamics of Zn(II) complexes with unstructured regions of Aspf2; basing on a variety of spectrometric and potentiometric data, we show that the C-terminal part has the highest Zn(II) binding affinity among the potential binding sites, and Ni(II) does not compete with Zn(II) binding to this region. The 14 amino acid Aspf2 C-terminus coordinates Zn(II) via two Cys thiolates and two His imidazoles and it could be considered as a promising A. fumigatus targeting molecule.

PMID:35700143 | DOI:10.1093/mtomcs/mfac042

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