View source for 6m97


==Crystal structure of the high-affinity copper transporter Ctr1==
<StructureSection load='6m97' size='340' side='right'caption='[[6m97]], [[Resolution|resolution]] 3.03&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6m97]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Salmo_salar Salmo salar]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6M97 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6M97 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.03&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6m97 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m97 OCA], [https://pdbe.org/6m97 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6m97 RCSB], [https://www.ebi.ac.uk/pdbsum/6m97 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6m97 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/C562_ECOLX C562_ECOLX] Electron-transport protein of unknown function.[https://www.uniprot.org/uniprot/C0HAK2_SALSA C0HAK2_SALSA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Copper (Cu) is an essential trace element for growth and development and abnormal Cu levels are associated with anemia, metabolic disease and cancer. Evolutionarily conserved from fungi to humans, the high-affinity Cu(+) transporter Ctr1 is crucial for both dietary Cu uptake and peripheral distribution, yet the mechanisms for selective permeation of potentially toxic Cu(+) ions across cell membranes are unknown. Here we present X-ray crystal structures of Ctr1 from Salmo salar in both Cu(+)-free and Cu(+)-bound states, revealing a homo-trimeric Cu(+)-selective ion channel-like architecture. Two layers of methionine triads form a selectivity filter, coordinating two bound Cu(+) ions close to the extracellular entrance. These structures, together with Ctr1 functional characterization, provide a high resolution picture to understand Cu(+) import across cellular membranes and suggest therapeutic opportunities for intervention in diseases characterized by inappropriate Cu accumulation.

X-ray structures of the high-affinity copper transporter Ctr1.,Ren F, Logeman BL, Zhang X, Liu Y, Thiele DJ, Yuan P Nat Commun. 2019 Mar 27;10(1):1386. doi: 10.1038/s41467-019-09376-7. PMID:30918258<ref>PMID:30918258</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6m97" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Salmo salar]]
[[Category: Ren F]]
[[Category: Yuan P]]