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Visualizing tricoordinate copper transfer

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Copper is a requisite cofactor in myriad cellular enzymes and is shuttled to different cellular sites for the assembly of copper-containing enzymes by Cu(I)-binding metallochaperones. NMR structural studies now reveal a key step in copper ion trafficking to sites of use.

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Figure 1: The tricoordinate Cu(I) thiolate intermediate of Atx1 (gold) and Ccc2a (blue).

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Cobine, P., Winge, D. Visualizing tricoordinate copper transfer. Nat Chem Biol 2, 352–353 (2006). https://doi.org/10.1038/nchembio0706-352

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