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| | <StructureSection load='5tsb' size='340' side='right'caption='[[5tsb]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='5tsb' size='340' side='right'caption='[[5tsb]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5tsb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Alcaligenes_bronchisepticus Alcaligenes bronchisepticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TSB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TSB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5tsb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bordetella_bronchiseptica_RB50 Bordetella bronchiseptica RB50]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TSB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TSB FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BB2405 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=257310 Alcaligenes bronchisepticus])</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=5tsb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tsb OCA], [https://pdbe.org/5tsb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tsb RCSB], [https://www.ebi.ac.uk/pdbsum/5tsb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tsb ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5tsb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tsb OCA], [http://pdbe.org/5tsb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tsb RCSB], [http://www.ebi.ac.uk/pdbsum/5tsb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tsb ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Alcaligenes bronchisepticus]] | + | [[Category: Bordetella bronchiseptica RB50]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Fellner, M]] | + | [[Category: Fellner M]] |
| - | [[Category: Hu, J]] | + | [[Category: Hu J]] |
| - | [[Category: Liu, J]] | + | [[Category: Liu J]] |
| - | [[Category: Sui, D]] | + | [[Category: Sui D]] |
| - | [[Category: Zhang, T]] | + | [[Category: Zhang T]] |
| - | [[Category: Binuclear metal center]]
| + | |
| - | [[Category: Cadmium]]
| + | |
| - | [[Category: Lipidic cubic phase]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Metal binding protein]]
| + | |
| - | [[Category: Transporter]]
| + | |
| - | [[Category: Zinc]]
| + | |
| - | [[Category: Zip]]
| + | |
| Structural highlights
Function
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+).[1]
Publication Abstract from PubMed
Zrt/Irt-like proteins (ZIPs) play fundamental roles in metal metabolism/homeostasis and are broadly involved in numerous physiological and pathological processes. The lack of high-resolution structure of the ZIPs hinders understanding of the metal transport mechanism. We report two crystal structures of a prokaryotic ZIP in lipidic cubic phase with bound metal substrates (Cd2+ at 2.7 A and Zn2+ at 2.4 A). The structures revealed a novel 3+2+3TM architecture and an inward-open conformation occluded at the extracellular side. Two metal ions were trapped halfway through the membrane, unexpectedly forming a binuclear metal center. The Zn2+-substituted structure suggested asymmetric functions of the two metal-binding sites and also revealed a route for zinc release. Mapping of disease-causing mutations, structure-guided mutagenesis, and cell-based zinc transport assay demonstrated the crucial role of the binuclear metal center for human ZIP4. A metal transport mechanism for the ZIP from Bordetella bronchiseptica was proposed, which is likely applicable to other ZIPs.
Crystal structures of a ZIP zinc transporter reveal a binuclear metal center in the transport pathway.,Zhang T, Liu J, Fellner M, Zhang C, Sui D, Hu J Sci Adv. 2017 Aug 25;3(8):e1700344. doi: 10.1126/sciadv.1700344. eCollection 2017, Aug. PMID:28875161[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lin W, Chai J, Love J, Fu D. Selective electrodiffusion of zinc ions in a Zrt-, Irt-like protein, ZIPB. J Biol Chem. 2010 Dec 10;285(50):39013-20. PMID:20876577 doi:10.1074/jbc.M110.180620
- ↑ Zhang T, Liu J, Fellner M, Zhang C, Sui D, Hu J. Crystal structures of a ZIP zinc transporter reveal a binuclear metal center in the transport pathway. Sci Adv. 2017 Aug 25;3(8):e1700344. doi: 10.1126/sciadv.1700344. eCollection 2017, Aug. PMID:28875161 doi:http://dx.doi.org/10.1126/sciadv.1700344
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