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New page: left|200px<br /><applet load="1fvs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fvs" /> '''SOLUTION STRUCTURE OF THE YEAST COPPER TRANS...
 
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[[Image:1fvs.gif|left|200px]]<br /><applet load="1fvs" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1fvs" />
'''SOLUTION STRUCTURE OF THE YEAST COPPER TRANSPORTER DOMAIN CCC2A IN THE APO AND CU(I) LOAD STATES'''<br />


==Overview==
==SOLUTION STRUCTURE OF THE YEAST COPPER TRANSPORTER DOMAIN CCC2A IN THE APO AND CU(I) LOAD STATES==
Ccc2 is an intracellular copper transporter in Saccharomyces cerevisiae, and is a physiological target of the copper chaperone Atx1. Here we, describe the solution structure of the first N-terminal MTCXXC, metal-binding domain, Ccc2a, both in the presence and absence of Cu(I)., For Cu(I)-Ccc2a, 1944 meaningful nuclear Overhauser effects were used to, obtain a family of 35 structures with root mean square deviation to the, average structure of 0.36 +/- 0.06 A for the backbone and 0.79 +/- 0.05 A, for the heavy atoms. For apo-Ccc2a, 1970 meaningful nuclear Overhauser, effects have been used with 35 (3)J(HNHalpha) to obtain a family of 35, structures with root mean square deviation to the average structure of, 0.38 +/- 0.06 A for the backbone and 0.82 +/- 0.07 A for the heavy atoms., The protein exhibits a betaalphabetabetaalphabeta, ferrodoxin-like fold, similar to that of its target Atx1 and that of a human counterpart, the, fourth metal-binding domain of the Menkes protein. The overall fold, remains unchanged upon copper loading, but the copper-binding site itself, becomes less disordered. The helical context of the copper-binding site, and the copper-induced conformational changes in Ccc2a differ from those, in Atx1. Ccc2a presents a conserved acidic surface which complements the, basic surface of Atx1 and a hydrophobic surface. These results open new, mechanistic aspects of copper transporter domains with physiological, copper donor and acceptor proteins.
<StructureSection load='1fvs' size='340' side='right'caption='[[1fvs]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1fvs]] is a 1 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=1FVS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FVS 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=CU:COPPER+(II)+ION'>CU</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=1fvs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fvs OCA], [https://pdbe.org/1fvs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fvs RCSB], [https://www.ebi.ac.uk/pdbsum/1fvs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fvs ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ATU2_YEAST ATU2_YEAST] Probably involved in copper transport and in the regulation of cellular copper level. Retrieves copper from the metallochaperone ATX1 and incorporates it into trans-Golgi vesicles.
== 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/fv/1fvs_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=1fvs ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Ccc2 is an intracellular copper transporter in Saccharomyces cerevisiae and is a physiological target of the copper chaperone Atx1. Here we describe the solution structure of the first N-terminal MTCXXC metal-binding domain, Ccc2a, both in the presence and absence of Cu(I). For Cu(I)-Ccc2a, 1944 meaningful nuclear Overhauser effects were used to obtain a family of 35 structures with root mean square deviation to the average structure of 0.36 +/- 0.06 A for the backbone and 0.79 +/- 0.05 A for the heavy atoms. For apo-Ccc2a, 1970 meaningful nuclear Overhauser effects have been used with 35 (3)J(HNHalpha) to obtain a family of 35 structures with root mean square deviation to the average structure of 0.38 +/- 0.06 A for the backbone and 0.82 +/- 0.07 A for the heavy atoms. The protein exhibits a betaalphabetabetaalphabeta, ferrodoxin-like fold similar to that of its target Atx1 and that of a human counterpart, the fourth metal-binding domain of the Menkes protein. The overall fold remains unchanged upon copper loading, but the copper-binding site itself becomes less disordered. The helical context of the copper-binding site, and the copper-induced conformational changes in Ccc2a differ from those in Atx1. Ccc2a presents a conserved acidic surface which complements the basic surface of Atx1 and a hydrophobic surface. These results open new mechanistic aspects of copper transporter domains with physiological copper donor and acceptor proteins.


==About this Structure==
Solution structure of the yeast copper transporter domain Ccc2a in the apo and Cu(I)-loaded states.,Banci L, Bertini I, Ciofi-Baffoni S, Huffman DL, O'Halloran TV J Biol Chem. 2001 Mar 16;276(11):8415-26. Epub 2000 Nov 16. PMID:11083871<ref>PMID:11083871</ref>
1FVS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with CU as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Hydrogen/potassium-exchanging_ATPase Hydrogen/potassium-exchanging ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.10 3.6.3.10] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FVS OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Solution structure of the yeast copper transporter domain Ccc2a in the apo and Cu(I)-loaded states., Banci L, Bertini I, Ciofi-Baffoni S, Huffman DL, O'Halloran TV, J Biol Chem. 2001 Mar 16;276(11):8415-26. Epub 2000 Nov 16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11083871 11083871]
</div>
[[Category: Hydrogen/potassium-exchanging ATPase]]
<div class="pdbe-citations 1fvs" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[ATPase 3D structures|ATPase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Banci L]]
[[Category: Baffoni, S.Ciofi.]]
[[Category: Bertini I]]
[[Category: Banci, L.]]
[[Category: Ciofi Baffoni S]]
[[Category: Bertini, I.]]
[[Category: Huffman DL]]
[[Category: Halloran, T.V.O.]]
[[Category: O'Halloran TV]]
[[Category: Huffman, D.L.]]
[[Category: CU]]
[[Category: babbab]]
[[Category: cu(i)-ccc2a]]
 
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