4x82

Crystal Structure of the Extracellular Domain of ZIP4

spinqualitylabelsall models 4x82, resolution 2.76Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4x82 is a 2 chain structure with sequence from Pteropus alecto. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.76Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function S39A4_PTEAL Selective transporter that mediates the uptake of Zn(2+) (PubMed:27321477). Plays an essential role for dietary zinc uptake from small intestine (By similarity). The Zn(2+) uniporter activity is regulated by zinc availability. Exhibits also polyspecific binding and transport of Cu(2+), Cd(2+) and possibly Ni(2+) but at higher concentrations (By similarity).[UniProtKB:Q6P5W5][UniProtKB:Q78IQ7] Publication Abstract from PubMed The ZIP zinc transporter family is responsible for zinc uptake from the extracellular milieu or intracellular vesicles. The LIV-1 subfamily, containing nine out of the 14 human ZIP proteins, is featured with a large extracellular domain (ECD). The critical role of the ECD is manifested by disease-causing mutations on ZIP4, a representative LIV-1 protein. Here we report the first crystal structure of a mammalian ZIP4-ECD, which reveals two structurally independent subdomains and an unprecedented dimer centred at the signature PAL motif. Structure-guided mutagenesis, cell-based zinc uptake assays and mapping of the disease-causing mutations indicate that the two subdomains play pivotal but distinct roles and that the bridging region connecting them is particularly important for ZIP4 function. These findings lead to working hypotheses on how ZIP4-ECD exerts critical functions in zinc transport. The conserved dimeric architecture in ZIP4-ECD is also demonstrated to be a common structural feature among the LIV-1 proteins. Structural insights of ZIP4 extracellular domain critical for optimal zinc transport.,Zhang T, Sui D, Hu J Nat Commun. 2016 Jun 20;7:11979. doi: 10.1038/ncomms11979. PMID:27321477 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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