Brief Communication abstract
Nature Chemical Biology 2, 367 - 368 (2006)
Published online: 28 May 2006 | doi:10.1038/nchembio797
The Atx1-Ccc2 complex is a metal-mediated protein-protein interaction
Lucia Banci1,2, Ivano Bertini1,2, Francesca Cantini1,2, Isabella C Felli1,2, Leonardo Gonnelli1, Nick Hadjiliadis1,3, Roberta Pierattelli1,2, Antonio Rosato1,2 & Petros Voulgaris1
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.
- Magnetic Resonance Center (CERM), University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, Italy.
- Department of Chemistry, University of Florence, Via della Lastruccia 3, 50019 Sesto Fiorentino, Italy.
- Section of Inorganic and Analytical Chemistry, Department of Chemistry, University of Ioannina, 45110 Ioannina, Greece.
Correspondence to: Ivano Bertini1,2 e-mail: ivanobertini@cerm.unifi.it
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