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5tsa

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Current revision (14:23, 6 March 2024) (edit) (undo)
 
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<StructureSection load='5tsa' size='340' side='right'caption='[[5tsa]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='5tsa' size='340' side='right'caption='[[5tsa]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5tsa]] 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=5TSA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TSA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5tsa]] 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=5TSA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TSA FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5tsb|5tsb]]</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=ZN:ZINC+ION'>ZN</scene></td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5tsa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tsa OCA], [https://pdbe.org/5tsa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tsa RCSB], [https://www.ebi.ac.uk/pdbsum/5tsa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tsa ProSAT]</span></td></tr>
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<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=5tsa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tsa OCA], [http://pdbe.org/5tsa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tsa RCSB], [http://www.ebi.ac.uk/pdbsum/5tsa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tsa ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A0A0H3LM39_BORBR A0A0H3LM39_BORBR]
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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.
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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<ref>PMID:28875161</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 5tsa" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Alcaligenes bronchisepticus]]
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[[Category: Bordetella bronchiseptica RB50]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Fellner, M]]
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[[Category: Fellner M]]
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[[Category: Hu, J]]
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[[Category: Hu J]]
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[[Category: Liu, J]]
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[[Category: Liu J]]
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[[Category: Sui, D]]
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[[Category: Sui D]]
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[[Category: Zhang, T]]
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[[Category: Zhang T]]
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[[Category: Binuclear metal centerzinc]]
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[[Category: Cadmium]]
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[[Category: Lipidic cubic phase]]
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[[Category: Metal binding protein]]
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[[Category: Transporter]]
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[[Category: Zinc]]
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[[Category: Zip]]
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Current revision

Crystal structure of the Zrt-/Irt-like protein from Bordetella bronchiseptica with bound Zn2+

PDB ID 5tsa

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OCA

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