5tsa: Difference between revisions
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==Crystal structure of the Zrt-/Irt-like protein from Bordetella bronchiseptica with bound Zn2+== | |||
<StructureSection load='5tsa' size='340' side='right' caption='[[5tsa]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5tsa]] is a 1 chain structure. 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> | |||
</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> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5tsb|5tsb]]</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=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> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:28875161</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5tsa" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Fellner, M]] | |||
[[Category: Hu, J]] | |||
[[Category: Liu, J]] | |||
[[Category: Sui, D]] | [[Category: Sui, D]] | ||
[[Category: Zhang, T]] | [[Category: Zhang, T]] | ||
[[Category: | [[Category: Binuclear metal centerzinc]] | ||
[[Category: | [[Category: Cadmium]] | ||
[[Category: Lipidic cubic phase]] | |||
[[Category: Metal binding protein]] | |||
[[Category: Transporter]] | |||
[[Category: Zinc]] | |||
[[Category: Zip]] | |||
Revision as of 04:44, 21 September 2017
Crystal structure of the Zrt-/Irt-like protein from Bordetella bronchiseptica with bound Zn2+
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