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báo cáo khoa hoc : Cu(I)- and proton-binding properties of the first N-terminal soluble domain of Bacillus subtilis CopA
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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, an arrangement that occurs widely in copper transporters from both prokaryotes and eukaryotes. Both domains were previously found to bind Cu(I) with very high affinity.
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