| Products/Services Used | Details | Operation |
|---|---|---|
| Proteins, Expression, Isolation and Analysis | Proteins were eluted with 20 µL of 100 mM Tris-HCl, 150 mM NaCl, 1 mM EDTA, and 2.5 mM desthiobiotin, pH 8.0, boiled for 5 min with SDS-sample buffer, and separated by SDS-PAGE (4-20% ExpressPlus™ PAGE Gel, Genscript), followed by immunoblotting. | Get A Quote |
Heme has a critical role in the chemical framework of the cell as an essential protein cofactor and signaling molecule that controls diverse processes and molecular interactions. Using a phylogenomics-based approach and complementary structural techniques, we identify a family of dimeric hemoproteins comprising a domain of unknown function DUF2470. The heme iron is axially coordinated by two zinc-bound histidine residues, forming a distinct two-fold symmetric zinc-histidine-iron-histidine-zinc site. Together with structure-guided in vitro and in vivo experiments, we further demonstrate the existence of a functional link between heme binding by Dri1 (Domain related to iron 1, formerly ssr1698) and post-translati... More
