5TSA
Crystal structure of the Zrt-/Irt-like protein from Bordetella bronchiseptica with bound Zn2+
Summary for 5TSA
| Entry DOI | 10.2210/pdb5tsa/pdb |
| Related | 5TSB |
| Descriptor | Membrane protein, ZINC ION, CADMIUM ION, ... (4 entities in total) |
| Functional Keywords | zip, transporter, zinc, cadmium, lipidic cubic phase, binuclear metal centerzinc, metal binding protein |
| Biological source | Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) |
| Total number of polymer chains | 1 |
| Total formula weight | 31514.16 |
| Authors | Zhang, T.,Fellner, M.,Sui, D.,Liu, J.,Hu, J. (deposition date: 2016-10-28, release date: 2017-09-20, Last modification date: 2024-04-03) |
| Primary citation | Zhang, T.,Liu, J.,Fellner, M.,Zhang, C.,Sui, D.,Hu, J. Crystal structures of a ZIP zinc transporter reveal a binuclear metal center in the transport pathway. Sci Adv, 3:e1700344-e1700344, 2017 Cited by PubMed Abstract: Zrt/Irt-like proteins (ZIPs) play fundamental roles in metal metabolism/homeostasis and are broadly involved in numerous physiological and pathological processes. The lack of high-resolution structure of the ZIPs hinders understanding of the metal transport mechanism. We report two crystal structures of a prokaryotic ZIP in lipidic cubic phase with bound metal substrates (Cd at 2.7 Å and Zn at 2.4 Å). The structures revealed a novel 3+2+3TM architecture and an inward-open conformation occluded at the extracellular side. Two metal ions were trapped halfway through the membrane, unexpectedly forming a binuclear metal center. The Zn-substituted structure suggested asymmetric functions of the two metal-binding sites and also revealed a route for zinc release. Mapping of disease-causing mutations, structure-guided mutagenesis, and cell-based zinc transport assay demonstrated the crucial role of the binuclear metal center for human ZIP4. A metal transport mechanism for the ZIP from was proposed, which is likely applicable to other ZIPs. PubMed: 28875161DOI: 10.1126/sciadv.1700344 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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