Structural highlights
Function
[ATX1_YEAST] Shuttles copper to the transport ATPase CCC2. Protects against oxygen toxicity. [ATU2_YEAST] Probably involved in copper transport and in the regulation of cellular copper level. Retrieves copper from the metallochaperone ATX1 and incorporates it into trans-Golgi vesicles.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.,Banci L, Bertini I, Cantini F, Felli IC, Gonnelli L, Hadjiliadis N, Pierattelli R, Rosato A, Voulgaris P Nat Chem Biol. 2006 Jul;2(7):367-8. Epub 2006 May 28. PMID:16732294[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Banci L, Bertini I, Cantini F, Felli IC, Gonnelli L, Hadjiliadis N, Pierattelli R, Rosato A, Voulgaris P. The Atx1-Ccc2 complex is a metal-mediated protein-protein interaction. Nat Chem Biol. 2006 Jul;2(7):367-8. Epub 2006 May 28. PMID:16732294 doi:10.1038/nchembio797
