PMID:12052259
| Citation |
Ahumada, A and Tse-Dinh, YC (2002) The role of the Zn(II) binding domain in the mechanism of E. coli DNA topoisomerase I. BMC Biochem. 3:13 |
|---|---|
| Abstract |
Escherichia 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. |
| Links | |
| Keywords |
Binding Sites; Catalytic Domain; DNA/chemistry; DNA/metabolism; DNA Topoisomerases, Type I/chemistry; DNA Topoisomerases, Type I/metabolism; DNA, Circular/metabolism; DNA, Single-Stranded/chemistry; DNA, Single-Stranded/metabolism; DNA, Superhelical/metabolism; Escherichia coli/enzymology; Magnesium/pharmacology; Models, Genetic; Protein Binding; Protein Structure, Tertiary; Sodium Chloride/pharmacology; Substrate Specificity; Zinc/metabolism |
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