Biochemical and Functional Evaluation of the Intramolecular Disulfide Bonds in the Zinc-Chelating Antimicrobial Protein Human S100A7 (Psoriasin).

ABSTRACT: Human S100A7 (psoriasin) is a metal-chelating protein expressed by epithelial cells. It is a 22-kDa homodimer with two EF-hand domains per subunit and two transition-metal-binding His₃Asp sites at the dimer interface. Each subunit contains two cysteine residues that can exist as free thiols (S100A7_red) or as an intramolecular disulfide bond (S100A7_ox). Herein, we examine the disulfide bond redox behavior, the Zn(II) binding properties, and the antibacterial activity of S100A7, as well as the effect of Ca(II) ions on these properties. In agreement with prior work [Hein, K. Z., et al. (2013) Proc. Natl. Acad. Sci. U. S. A. 112, 13039-13044], we show that apo S100A7_ox is a substrate for the mammalian thioredoxin system; however, negligible reduction

SUBMITTER: Cunden LS 

PROVIDER: S-EPMC5748159 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature