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1fvq

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[[Image:1fvq.gif|left|200px]]
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{{STRUCTURE_1fvq| PDB=1fvq | SCENE= }}
{{STRUCTURE_1fvq| PDB=1fvq | SCENE= }}
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'''SOLUTION STRUCTURE OF THE YEAST COPPER TRANSPORTER DOMAIN CCC2A IN THE APO AND CU(I) LOADED STATES'''
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===SOLUTION STRUCTURE OF THE YEAST COPPER TRANSPORTER DOMAIN CCC2A IN THE APO AND CU(I) LOADED STATES===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11083871 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11083871}}
==About this Structure==
==About this Structure==
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1FVQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FVQ OCA].
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1FVQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FVQ OCA].
==Reference==
==Reference==
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[[Category: Huffman, D L.]]
[[Category: Huffman, D L.]]
[[Category: Apo-ccc2a]]
[[Category: Apo-ccc2a]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:49:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:00:49 2008''

Revision as of 01:00, 1 July 2008

Image:1fvq.png

Template:STRUCTURE 1fvq

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

Template:ABSTRACT PUBMED 11083871

About this Structure

1FVQ is a Single protein structure of sequence from Saccharomyces cerevisiae. Full experimental information is available from OCA.

Reference

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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