1fvq
From Proteopedia
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| - | [[Image:1fvq.gif|left|200px]] | + | [[Image:1fvq.gif|left|200px]] |
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| - | '''SOLUTION STRUCTURE OF THE YEAST COPPER TRANSPORTER DOMAIN CCC2A IN THE APO AND CU(I) LOADED STATES''' | + | {{Structure |
| + | |PDB= 1fvq |SIZE=350|CAPTION= <scene name='initialview01'>1fvq</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''SOLUTION STRUCTURE OF THE YEAST COPPER TRANSPORTER DOMAIN CCC2A IN THE APO AND CU(I) LOADED STATES''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1FVQ is a [ | + | 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]. |
==Reference== | ==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:[http:// | + | 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://www.ncbi.nlm.nih.gov/pubmed/11083871 11083871] |
[[Category: Hydrogen/potassium-exchanging ATPase]] | [[Category: Hydrogen/potassium-exchanging ATPase]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
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[[Category: apo-ccc2a]] | [[Category: apo-ccc2a]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:14:38 2008'' |
Revision as of 09:14, 20 March 2008
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| Activity: | Hydrogen/potassium-exchanging ATPase, with EC number 3.6.3.10 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SOLUTION STRUCTURE OF THE YEAST COPPER TRANSPORTER DOMAIN CCC2A IN THE APO AND CU(I) LOADED STATES
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.
About this Structure
1FVQ is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic 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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