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PDBsum entry 1ecl
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Topoisomerase
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PDB id
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1ecl
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References listed in PDB file
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Key reference
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Title
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Three-Dimensional structure of the 67k n-Terminal fragment of e. Coli DNA topoisomerase i.
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Authors
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C.D.Lima,
J.C.Wang,
A.Mondragón.
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Ref.
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Nature, 1994,
367,
138-146.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 2.
FIG 2. Overall architecture.
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Figure 5.
FIG 5. Proposed steps in the strand passage reaction.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nature
(1994,
367,
138-146)
copyright 1994.
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Secondary reference #1
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Title
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Crystallization of a 67 kda fragment of escherichia coli DNA topoisomerase i.
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Authors
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C.D.Lima,
J.C.Wang,
A.Mondragón.
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Ref.
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J Mol Biol, 1993,
232,
1213-1216.
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PubMed id
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