The Atx1-Ccc2 complex is a metal-mediated protein-protein interaction.
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.
Banci
Lucia
L
Magnetic Resonance Center (CERM), University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, Italy.
Bertini
Ivano
I
Cantini
Francesca
F
Felli
Isabella C
IC
Gonnelli
Leonardo
L
Hadjiliadis
Nick
N
Pierattelli
Roberta
R
Rosato
Antonio
A
Voulgaris
Petros
P
D002352:Carrier Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D027682:Cation Transport Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D003300:Copper / Q000737:chemistry* / Q000378:metabolism*; D000079922:Copper Transport Proteins; D008024:Ligands; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D011485:Protein Binding; D020836:Protein Structure, Quaternary; D012441:Saccharomyces cerevisiae / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
C093341:ATX1 protein, S cerevisiae; C092974:CCC2 protein, S cerevisiae; D002352:Carrier Proteins; D027682:Cation Transport Proteins; D000079922:Copper Transport Proteins; D008024:Ligands; D029701:Saccharomyces cerevisiae Proteins; D003300:Copper