8ght: Difference between revisions
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==Cryo-electron microscopy structure of the zinc transporter from Bordetella bronchiseptica== | |||
<StructureSection load='8ght' size='340' side='right'caption='[[8ght]], [[Resolution|resolution]] 3.05Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8ght]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bordetella_bronchiseptica Bordetella bronchiseptica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8GHT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8GHT FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=PTY:PHOSPHATIDYLETHANOLAMINE'>PTY</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=8ght FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ght OCA], [https://pdbe.org/8ght PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ght RCSB], [https://www.ebi.ac.uk/pdbsum/8ght PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ght ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0H3LM39_BORBR A0A0H3LM39_BORBR] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Zinc is an essential micronutrient that supports all living organisms through regulating numerous biological processes. However, the mechanism of uptake regulation by intracellular Zn(2+) status remains unclear. Here we report a cryo-electron microscopy structure of a ZIP-family transporter from Bordetella bronchiseptica at 3.05 A resolution in an inward-facing, inhibited conformation. The transporter forms a homodimer, each protomer containing nine transmembrane helices and three metal ions. Two metal ions form a binuclear pore structure, and the third ion is located at an egress site facing the cytoplasm. The egress site is covered by a loop, and two histidine residues on the loop interact with the egress-site ion and regulate its release. Cell-based Zn(2+) uptake and cell growth viability assays reveal a negative regulation of Zn(2+) uptake through sensing intracellular Zn(2+) status using a built-in sensor. These structural and biochemical analyses provide mechanistic insight into the autoregulation of zinc uptake across membranes. | |||
Structural mechanism of intracellular autoregulation of zinc uptake in ZIP transporters.,Pang C, Chai J, Zhu P, Shanklin J, Liu Q Nat Commun. 2023 Jun 9;14(1):3404. doi: 10.1038/s41467-023-39010-6. PMID:37296139<ref>PMID:37296139</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8ght" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bordetella bronchiseptica]] | |||
[[Category: Large Structures]] | |||
[[Category: Chai J]] | |||
[[Category: Liu Q]] | |||
[[Category: Pang CX]] | |||
[[Category: Shanklin J]] | |||
Revision as of 09:39, 21 June 2023
Cryo-electron microscopy structure of the zinc transporter from Bordetella bronchiseptica
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