3iwp
From Proteopedia
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==Crystal structure of human copper homeostasis protein CutC== | ==Crystal structure of human copper homeostasis protein CutC== | ||
| - | <StructureSection load='3iwp' size='340' side='right' caption='[[3iwp]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='3iwp' size='340' side='right'caption='[[3iwp]], [[Resolution|resolution]] 2.50Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3iwp]] is a 12 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3iwp]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IWP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IWP FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3iwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3iwp OCA], [https://pdbe.org/3iwp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3iwp RCSB], [https://www.ebi.ac.uk/pdbsum/3iwp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3iwp ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/CUTC_HUMAN CUTC_HUMAN] May play a role in copper homeostasis. Can bind one Cu(1+) per subunit.<ref>PMID:16182249</ref> <ref>PMID:19878721</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iw/3iwp_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iw/3iwp_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3iwp ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3iwp ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Copper is an essential trace element to life and particularly plays a pivotal role in the physiology of aerobic organisms. The Cut protein family is associated with copper homeostasis and involved in uptake, storage, delivery, and efflux of copper. CutC is a member of the Cut family and is suggested to be involved in efflux trafficking of cuprous ion. We report here the biochemical and structural characterization of human CutC (hCutC). hCutC can bind Cu(I) with a stoichiometry of 1:1 and an apparent dissociation constant of 15.5+/-2.8 microM. hCutC assumes a typical TIM-barrel fold and forms a tetramer in both crystal structure and solution which is different from the dimeric architecture of the bacterial CutC. Structure analysis and sequence comparison of CutC proteins from different species reveal two strictly conserved Cys residues on the inner surface of the C-terminal end of the TIM-barrel. Mutations of the two Cys residues can significantly impair the binding ability of hCutC with Cu(I). Our results suggest that hCutC functions as an enzyme with Cu(I) as a cofactor rather than a copper transporter and the potential Cu(I)-binding site consists of the two Cys residues and other conserved residues in the vicinity. | ||
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| + | Crystal structure of human copper homeostasis protein CutC reveals a potential copper-binding site.,Li Y, Du J, Zhang P, Ding J J Struct Biol. 2010 Mar;169(3):399-405. doi: 10.1016/j.jsb.2009.10.012. Epub 2009, Oct 28. PMID:19878721<ref>PMID:19878721</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3iwp" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
| - | [[Category: Ding | + | [[Category: Large Structures]] |
| - | [[Category: Du | + | [[Category: Ding J]] |
| - | [[Category: Li | + | [[Category: Du J]] |
| - | [[Category: Zhang | + | [[Category: Li Y]] |
| - | + | [[Category: Zhang P]] | |
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Current revision
Crystal structure of human copper homeostasis protein CutC
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Categories: Homo sapiens | Large Structures | Ding J | Du J | Li Y | Zhang P
