View source for 2ggp


==Solution structure of the Atx1-Cu(I)-Ccc2a complex==
<StructureSection load='2ggp' size='340' side='right'caption='[[2ggp]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2ggp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GGP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GGP FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</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=2ggp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ggp OCA], [https://pdbe.org/2ggp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ggp RCSB], [https://www.ebi.ac.uk/pdbsum/2ggp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ggp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ATX1_YEAST ATX1_YEAST] Shuttles copper to the transport ATPase CCC2. Protects against oxygen toxicity.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gg/2ggp_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </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=2ggp ConSurf].
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== Publication Abstract from PubMed ==
Cellular systems allow transition-metal ions to reach or leave the cell or intracellular locations through metal transfer between proteins. By coupling mutagenesis and advanced NMR experiments, we structurally characterized the adduct between the copper chaperone Atx1 and the first copper(I)-binding domain of the Ccc2 ATPase. Copper was required for the interaction. This study provides an understanding of metal-mediated protein-protein interactions in which the metal ion is essential for the weak, reversible interaction between the partners.

The Atx1-Ccc2 complex is a metal-mediated protein-protein interaction.,Banci L, Bertini I, Cantini F, Felli IC, Gonnelli L, Hadjiliadis N, Pierattelli R, Rosato A, Voulgaris P Nat Chem Biol. 2006 Jul;2(7):367-8. Epub 2006 May 28. PMID:16732294<ref>PMID:16732294</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2ggp" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Banci L]]
[[Category: Bertini I]]
[[Category: Cantini F]]
[[Category: Felli IC]]
[[Category: Gonnelli L]]
[[Category: Hadjiliadis N]]
[[Category: Pierattelli R]]
[[Category: Rosato A]]
[[Category: Voulgaris P]]