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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"  
[[Image:1fvs.gif|left|200px]]<br /><applet load="1fvs" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1fvs" />
caption="1fvs" />
'''SOLUTION STRUCTURE OF THE YEAST COPPER TRANSPORTER DOMAIN CCC2A IN THE APO AND CU(I) LOAD STATES'''<br />
'''SOLUTION STRUCTURE OF THE YEAST COPPER TRANSPORTER DOMAIN CCC2A IN THE APO AND CU(I) LOAD STATES'''<br />


==Overview==
==Overview==
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.
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==
==About this Structure==
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].  
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 <scene name='pdbligand=CU:'>CU</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1FVS OCA].  


==Reference==
==Reference==
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Baffoni, S.Ciofi.]]
[[Category: Baffoni, S Ciofi.]]
[[Category: Banci, L.]]
[[Category: Banci, L.]]
[[Category: Bertini, I.]]
[[Category: Bertini, I.]]
[[Category: Halloran, T.V.O.]]
[[Category: Halloran, T V.O.]]
[[Category: Huffman, D.L.]]
[[Category: Huffman, D L.]]
[[Category: CU]]
[[Category: CU]]
[[Category: babbab]]
[[Category: babbab]]
[[Category: cu(i)-ccc2a]]
[[Category: cu(i)-ccc2a]]


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