8j80 | pdb_00008j80

Cryo-EM structure of hZnT7-Fab complex in zinc state 1, determined in heterogeneous conformations- one subunit in an inward-facing zinc-bound and the other in an outward-facing zinc-unbound conformation

spinqualitylabelsall models 8j80, resolution 2.68Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8j80 is a 6 chain structure with sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.68Å Ligands: ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease ZNT7_HUMAN The disease may be caused by variants affecting the gene represented in this entry. Function ZNT7_HUMAN Zinc ion transporter mediating zinc entry from the cytosol into the lumen of organelles along the secretory pathway (PubMed:15525635, PubMed:15994300). By contributing to zinc ion homeostasis within the early secretory pathway, regulates the activation and folding of enzymes like alkaline phosphatases (PubMed:15525635, PubMed:15994300). Publication Abstract from PubMed Zinc ions (Zn(2+)) are vital to most cells, with the intracellular concentrations of Zn(2+) being tightly regulated by multiple zinc transporters located at the plasma and organelle membranes. We herein present the 2.2-3.1 A-resolution cryo-EM structures of a Golgi-localized human Zn(2+)/H(+) antiporter ZnT7 (hZnT7) in Zn(2+)-bound and unbound forms. Cryo-EM analyses show that hZnT7 exists as a dimer via tight interactions in both the cytosolic and transmembrane (TM) domains of two protomers, each of which contains a single Zn(2+)-binding site in its TM domain. hZnT7 undergoes a TM-helix rearrangement to create a negatively charged cytosolic cavity for Zn(2+) entry in the inward-facing conformation and widens the luminal cavity for Zn(2+) release in the outward-facing conformation. An exceptionally long cytosolic histidine-rich loop characteristic of hZnT7 binds two Zn(2+) ions, seemingly facilitating Zn(2+) recruitment to the TM metal transport pathway. These structures permit mechanisms of hZnT7-mediated Zn(2+) uptake into the Golgi to be proposed. Cryo-EM structures of human zinc transporter ZnT7 reveal the mechanism of Zn(2+) uptake into the Golgi apparatus.,Bui HB, Watanabe S, Nomura N, Liu K, Uemura T, Inoue M, Tsutsumi A, Fujita H, Kinoshita K, Kato Y, Iwata S, Kikkawa M, Inaba K Nat Commun. 2023 Aug 8;14(1):4770. doi: 10.1038/s41467-023-40521-5. PMID:37553324 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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