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pubmed-article:12052259pubmed:abstractTextEscherichia coli DNA topoisomerase I binds three Zn(II) with three tetracysteine motifs which, together with the 14 kDa C-terminal region, form a 30 kDa DNA binding domain (ZD domain). The 67 kDa N-terminal domain (Top67) has the active site tyrosine for DNA cleavage but cannot relax negatively supercoiled DNA. We analyzed the role of the ZD domain in the enzyme mechanism.lld:pubmed
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pubmed-article:12052259pubmed:authorpubmed-author:AhumadaAdrian...lld:pubmed
pubmed-article:12052259pubmed:authorpubmed-author:Tse-DinhYuk-C...lld:pubmed
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pubmed-article:12052259pubmed:dateRevised2010-11-18lld:pubmed
pubmed-article:12052259pubmed:articleTitleThe role of the Zn(II) binding domain in the mechanism of E. coli DNA topoisomerase I.lld:pubmed
pubmed-article:12052259pubmed:affiliationDepartment of Biochemistry and Molecular Biology, New York Medical College, Valhalla, NY, USA. a_ahumada@msn.comlld:pubmed
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