8ght

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== Structural highlights ==
== 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>
<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>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.05&#8491;</td></tr>
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<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>
<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>
</table>
== Function ==
== Function ==
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[https://www.uniprot.org/uniprot/A0A0H3LM39_BORBR A0A0H3LM39_BORBR]
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[https://www.uniprot.org/uniprot/ZIP_BORBR ZIP_BORBR] Selective electrodiffusional channel that mediates the uptake of Zn(2+). Exploits in vivo zinc concentration gradients (maintained by cellular zinc homeostasis) to passively move zinc ions into the cytoplasm. ZIPB-mediated zinc flux is dependent upon pH, but independent of the proton motive force. Is also able to import Cd(2+), but is not permeable to Co(2+), Cu(2+), Fe(2+), Mn(2+) and Ni(2+).<ref>PMID:20876577</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 8ght" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>

Current revision

Cryo-electron microscopy structure of the zinc transporter from Bordetella bronchiseptica

PDB ID 8ght

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