View source for 8j80


==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==
<StructureSection load='8j80' size='340' side='right'caption='[[8j80]], [[Resolution|resolution]] 2.68&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8j80]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8J80 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8J80 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.68&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8j80 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8j80 OCA], [https://pdbe.org/8j80 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8j80 RCSB], [https://www.ebi.ac.uk/pdbsum/8j80 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8j80 ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/ZNT7_HUMAN ZNT7_HUMAN] The disease may be caused by variants affecting the gene represented in this entry.
== Function ==
[https://www.uniprot.org/uniprot/ZNT7_HUMAN 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).<ref>PMID:15525635</ref> <ref>PMID:15994300</ref> 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:37553324</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8j80" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Han BB]]
[[Category: Inaba K]]
[[Category: Watanabe S]]