Structural mechanism of intracellular autoregulation of zinc uptake in ZIP transporters.

ABSTRACT: Zinc is an essential micronutrient that supports all living organisms through regulating numerous biological processes. However, the mechanism of uptake regulation by intracellular Zn²⁺ status remains unclear. Here we report a cryo-electron microscopy structure of a ZIP-family transporter from Bordetella bronchiseptica at 3.05 Å resolution in an inward-facing, inhibited conformation. The transporter forms a homodimer, each protomer containing nine transmembrane helices and three metal ions. Two metal ions form a binuclear pore structure, and the third ion is located at an egress site facing the cytoplasm. The egress site is covered by a loop, and two histidine residues on the loop interact with the egress-site ion and regulate its release. Cell-based Zn²⁺ uptake and c

SUBMITTER: Pang C 

PROVIDER: S-EPMC10256678 | biostudies-literature | 2023 Jun

REPOSITORIES: biostudies-literature