8ght | pdb_00008ght

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

spinqualitylabelsall models 8ght, resolution 3.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8ght is a 2 chain structure with sequence from Bordetella bronchiseptica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CD, PTY Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0H3LM39_BORBR Publication Abstract from PubMed Zinc is an essential micronutrient that supports all living organisms through regulating numerous biological processes. However, the mechanism of uptake regulation by intracellular Zn(2+) status remains unclear. Here we report a cryo-electron microscopy structure of a ZIP-family transporter from Bordetella bronchiseptica at 3.05 A 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(2+) uptake and cell growth viability assays reveal a negative regulation of Zn(2+) uptake through sensing intracellular Zn(2+) status using a built-in sensor. These structural and biochemical analyses provide mechanistic insight into the autoregulation of zinc uptake across membranes. Structural mechanism of intracellular autoregulation of zinc uptake in ZIP transporters.,Pang C, Chai J, Zhu P, Shanklin J, Liu Q Nat Commun. 2023 Jun 9;14(1):3404. doi: 10.1038/s41467-023-39010-6. PMID:37296139 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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