2ggp

Solution structure of the Atx1-Cu(I)-Ccc2a complexSolution structure of the Atx1-Cu(I)-Ccc2a complex

Structural highlights 2ggp is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Ligands: Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ATX1_YEAST Shuttles copper to the transport ATPase CCC2. Protects against oxygen toxicity. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 2ggp Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image