1fvq: Difference between revisions

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SOLUTION STRUCTURE OF THE YEAST COPPER TRANSPORTER DOMAIN CCC2A IN THE APO AND CU(I) LOADED STATES

OverviewOverview

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 StructureAbout this Structure

1FVQ is a Single protein structure of sequence from Saccharomyces cerevisiae. Active as Hydrogen/potassium-exchanging ATPase, with EC number 3.6.3.10 Full crystallographic information is available from OCA.

ReferenceReference

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

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-[[Image:1fvq.gif|left|200px]]<br /><applet load="1fvq" size="450" color="white" frame="true" align="right" spinBox="true"
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 '''SOLUTION STRUCTURE OF THE YEAST COPPER TRANSPORTER DOMAIN CCC2A IN THE APO AND CU(I) LOADED STATES'''<br />
 ==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==
-FVQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. 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=1FVQ OCA].
+FVQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. 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=1FVQ OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Saccharomyces cerevisiae]]
 [[Category: Single protein]]
-[[Category: Baffoni, S.Ciofi.]]
+[[Category: Baffoni, S Ciofi.]]
 [[Category: Banci, L.]]
 [[Category: Bertini, I.]]
-[[Category: Halloran, T.V.O.]]
+[[Category: Halloran, T V.O.]]
-[[Category: Huffman, D.L.]]
+[[Category: Huffman, D L.]]
 [[Category: apo-ccc2a]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:20:37 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:43:11 2008''