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Liang Zhou, Chloe Singleton, Oliver Hecht, Geoffrey R. Moore and Nick E. Le Brun Cu(I)- and proton-binding properties of the first N-terminal soluble domain of Bacillus subtilis CopA The FEBS Journal 279

Version of Record online: 6 DEC 2011 | DOI: 10.1111/j.1742-4658.2011.08422.x

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CopA, a P-type ATPase transporter involved in copper detoxification in Bacillus subtilis, contains two soluble Atx1-like domains separated by a short linker at its N-terminus. Here, the first soluble domain in isolation, CopAa, was found to exhibit complex high affinity Cu(I)-binding behaviour involving multiple ions and protein association. These properties are distinct from those of the two domain protein CopAab.

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