2GGP: Solution structure of the Atx1-Cu(I)-Ccc2a complex

Citation:
Abstract
Cellular systems allow transition-metal ions to reach or leave the cell or intracellular locations through metal transfer between proteins. By coupling mutagenesis and advanced NMR experiments, we structurally characterized the adduct between the copper chaperone Atx1 and the first copper(I)-binding domain of the Ccc2 ATPase. Copper was required for the interaction. This study provides an understanding of metal-mediated protein-protein interactions in which the metal ion is essential for the weak, reversible interaction between the partners.
PDB ID: 2GGPDownload
MMDB ID: 40917
PDB Deposition Date: 2006/3/24
Updated in MMDB: 2012/12
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Molecular Components in 2GGP
Label Count Molecule
Proteins (2 molecules)
1
Metal Homeostasis Factor Atx1(Gene symbol: ATX1)
Molecule annotation
1
Probable Copper-transporting Atpase(Gene symbol: CCC2)
Molecule annotation
Chemical (1 molecule)
1
1
* Click molecule labels to explore molecular sequence information.

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