8GHT

Cryo-electron microscopy structure of the zinc transporter from Bordetella bronchiseptica

Summary for 8GHT

• Entry DOI: 10.2210/pdb8ght/pdb
• EMDB information: 40050
• Descriptor: Putative membrane protein, CADMIUM ION, PHOSPHATIDYLETHANOLAMINE (3 entities in total)
• Functional Keywords: zinc transporter, dimer, complex, metal binding, inward-open inhibited conformation, transport protein
• Biological source: Bordetella bronchiseptica
• Total number of polymer chains: 2
• Total formula weight: 64725.68

Authors

Liu, Q.,Chai, J.,Pang, C.X.,Shanklin, J. (deposition date: 2023-03-12, release date: 2023-06-21, Last modification date: 2024-06-19)

Primary citation

Pang, C.,Chai, J.,Zhu, P.,Shanklin, J.,Liu, Q.
Structural mechanism of intracellular autoregulation of zinc uptake in ZIP transporters.
Nat Commun, 14:3404-3404, 2023

PubMed Abstract: Zinc is an essential micronutrient that supports all living organisms through regulating numerous biological processes. However, the mechanism of uptake regulation by intracellular Zn 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 Zn uptake and cell growth viability assays reveal a negative regulation of Zn uptake through sensing intracellular Zn status using a built-in sensor. These structural and biochemical analyses provide mechanistic insight into the autoregulation of zinc uptake across membranes.

PubMed: 37296139
DOI: 10.1038/s41467-023-39010-6

Experimental method

ELECTRON MICROSCOPY (3.05 Å)