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.
The Atx1-Ccc2 complex is a metal-mediated protein-protein interaction / L.Banci; I.Bertini; F.Cantini; I.C.Felli; L.Gonnelli; N.Hadjiliadis; R.Pierattelli; A.Rosato; P.Voulgaris. - In: NATURE CHEMICAL BIOLOGY. - ISSN 1552-4450. - STAMPA. - 2:(2006), pp. 367-368. [10.1038/nchembio797]
The Atx1-Ccc2 complex is a metal-mediated protein-protein interaction
BANCI, LUCIA;BERTINI, IVANO;CANTINI, FRANCESCA;FELLI, ISABELLA CATERINA;GONNELLI, LEONARDO;PIERATTELLI, ROBERTA;ROSATO, ANTONIO;
2006
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.
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