2ggp
From Proteopedia
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Solution structure of the Atx1-Cu(I)-Ccc2a complex
Overview
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.
About this Structure
2GGP is a Protein complex structure of sequences from Saccharomyces cerevisiae with as ligand. Active as Copper-exporting ATPase, with EC number 3.6.3.4 Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 17:31:31 2008
Categories: Copper-exporting ATPase | Protein complex | Saccharomyces cerevisiae | Banci, L. | Bertini, I. | Cantini, F. | Felli, I C. | Gonnelli, L. | Hadjiliadis, N. | Pierattelli, R. | Rosato, A. | SPINE, Structural Proteomics in Europe. | Voulgaris, P. | CU1 | Complex | Copper transport | Nmr | Spine | Structural genomics | Structural proteomics in europe
