5tsa | pdb_00005tsa

Crystal structure of the Zrt-/Irt-like protein from Bordetella bronchiseptica with bound Zn2+

spinqualitylabelsall models 5tsa, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5tsa is a 1 chain structure with sequence from Alcaligenes bronchisepticus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CD, ZN Related: 5tsb Gene: BB2405 (Alcaligenes bronchisepticus) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 (Cd2+ at 2.7 A and Zn2+ at 2.4 A). 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 Zn2+-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 Bordetella bronchiseptica was proposed, which is likely applicable to other ZIPs. Crystal structures of a ZIP zinc transporter reveal a binuclear metal center in the transport pathway.,Zhang T, Liu J, Fellner M, Zhang C, Sui D, Hu J Sci Adv. 2017 Aug 25;3(8):e1700344. doi: 10.1126/sciadv.1700344. eCollection 2017, Aug. PMID:28875161 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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