Structural highlights
Evolutionary Conservation
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Publication Abstract from PubMed
The three-dimensional structure of the 67K amino-terminal fragment of Escherichia coli DNA topoisomerase I has been determined to 2.2 A resolution. The polypeptide folds in an unusual way to give four distinct domains enclosing a hole large enough to accommodate a double-stranded DNA. The active-site tyrosyl residue, which is involved in the transient breakage of a DNA strand and the formation of a covalent enzyme-DNA intermediate, is present at the interface of two domains. The structure suggests a plausible mechanism by which E. coli DNA topoisomerase I and other members of the same DNA topoisomerase subfamily could catalyse the passage of one DNA strand through a transient break in another strand.
Three-dimensional structure of the 67K N-terminal fragment of E. coli DNA topoisomerase I.,Lima CD, Wang JC, Mondragon A Nature. 1994 Jan 13;367(6459):138-46. PMID:8114910[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lima CD, Wang JC, Mondragon A. Three-dimensional structure of the 67K N-terminal fragment of E. coli DNA topoisomerase I. Nature. 1994 Jan 13;367(6459):138-46. PMID:8114910 doi:http://dx.doi.org/10.1038/367138a0
