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-Structure paper
タイトル | Structural mechanism of intracellular autoregulation of zinc uptake in ZIP transporters. |
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ジャーナル・号・ページ | Nat Commun, Vol. 14, Issue 1, Page 3404, Year 2023 |
掲載日 | 2023年6月9日 |
著者 | Changxu Pang / Jin Chai / Ping Zhu / John Shanklin / Qun Liu / |
PubMed 要旨 | 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 ...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. |
リンク | Nat Commun / PubMed:37296139 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.05 Å |
構造データ | EMDB-40050, PDB-8ght: |
化合物 | ChemComp-CD: ChemComp-PTY: |
由来 |
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キーワード | TRANSPORT PROTEIN / zinc transporter / dimer / complex / metal binding / inward-open inhibited conformation |