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DNA topoisomerases
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Reprinted from, Cold Spring Harbor Laboratory Press
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Nucleases
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Wang1
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DNA topoisomerases: why so many?
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Wang1
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Three-dimensional structure of the 67K N-terminal fragment of E. coli DNA topoisomerase I
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of outstanding interest, The structure of the 67 kDa fragment of E. coli DNA topoisomerase I shows a novel architecture in which a single polypeptide chain forms a toroidal structure. The location of the active site at the interface of two domains and the large hole in the protein suggest that the protein must undergo a large conformational change in order to perform its function. A possible mechanism of action consistent with the structural, mechanistic and biochemical data is suggested.
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(1994)
Nature
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Lima1
Wang2
Mondragón3
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10
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0028774040
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Crystal structure of amino terminal fragment of vaccinia virus topoisomerase I at 1.6 AA resolution
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of outstanding interest, The structure of a 9 kDa fragment of the N-terminal domain of Vaccinia virus DNA topoisomerase I represents the first structural information on any viral or eukaryotic-like topoisomerase. The structure shows that putative conserved residues amongst eukaryotic-like type I DNA topoisomerases do not map to any particular region of the protein. These findings suggest that the viral and eukaryotic type I protein may be less similar than previously thought.
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(1994)
Structure
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Sharma1
Hanai2
Mondragón3
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11
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Interaction between DNA and an Escherichia coli protein
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Escherichia coli DNA topoisomerase I is a zinc metalloprotein with three repetitive zinc-binding domains
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Tse-Dihn1
Beran-Seed2
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14
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Zinc(II) coordination in Escherichia coli: DNA topoisomerase I is required for cleavable complex formation with DNA
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Tse-Dinh1
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Probing the structural domains and function in vivo of Escherichia coli DNA topoisomerase I by mutagenesis
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(1986)
J Mol Biol
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Zumstein1
Wang2
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17
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Crystallization of a 67 kDa fragment of Escherichia coli DNA topoisomerase I
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Structural basis for the 3′–5′ exonuclease activity of Escherichia coli DNA polymerase I: a two metal ion mechanism
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Beese1
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23
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Cleavage of dT8 and dT8 phosphorothioyl analogues by Escherichia coli DNA topoisomerase I: product and rate analysis
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Biochemistry
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Domanico1
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24
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Catenation and knotting of duplex DNA by type 1 topoisomerases: a mechanistic parallel with type 2 topoisomerases
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(1981)
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Brown1
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25
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E. coli and M. luteus DNA topoisomerase I can catalyze catenation or decatenation of double-stranded DNA rings
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Vaccinia virus encapsidates a novel topoisomerase with the properties of a eukaryotic type I enzyme
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Shaffer1
Traktman2
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30
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Peptide sequencing and site directed mutagenesis identify tyrosine 727 as the active site tyrosine of Saccharomyces cerevisiae DNA topoisomerase I
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(1989)
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Lynn1
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31
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Specific DNA cleavage and binding by Vaccinia virus DNA topoisomerase I
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Shuman1
Prescott2
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32
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Vaccinia DNA topoisomerase I: single turnover and steady-state kinetic analysis of the DNA strand cleavage and ligation reactions
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of special interest, A thorough kinetic analysis of the cleavage and religation reaction of Vaccinia virus DNA topoisomerase I. This represents the most complete analysis of the cleavage/ligation reaction of any DNA topoisomerase. Vaccinia virus DNA topoisomerase I offered the opportunity to perform such an analysis because of its uniqueness in being a DNA sequence specific topoisomerase.
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Biochemistry
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Stivers1
Shuman2
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33
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DNA strand transfer reactions catalyzed by vaccinia topoisomerase I
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Tandem regions of yeast DNA topoisomerase II share homology with different subunits of bacterial gyrase
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Science
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Lynn1
Giaever2
Swanberg3
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37
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0028334718
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DNA transport by a type II DNA topoisomerase: evidence in favor of a two-gate mechanism
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of special interest, A study of the mechanism of action of yeast DNA topoisomerase II. By using a non-hydrolyzable ATP analog, the authors studied the catenation reaction and found that DNA molecules were captured inside the protein. The trapped products suggest that the protein functions through a two-gate mechanisms: the DNA molecule enters through one gate and exits through a second gate.
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(1994)
Cell
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Roca1
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38
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The capture of a DNA double helix by an ATP-dependent protein clamp: a key step in DNA transport by type II DNA topoisomerases
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(1992)
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Roca1
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39
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0025838305
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Proteolysis patterns of epitopically labeled yeast DNA toposiomerase II suggest an allosteric transition in the enzyme induced by ATP binding
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Proc Natl Acad Sci USA
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Lindsley1
Wang2
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40
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On the coupling between ATP usage and DNA transport by yeast DNA topoisomerase II
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DNA gyrase and its complexes with DNA: direct observation by electron microscopy
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Kirchhausen1
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44
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The 24 kDa N-terminal sub-domain of the DNA gyrase B protein binds coumarin drugs
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(1994)
Mol Microbiol
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Gilbert1
Maxwell2
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45
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Tryptic fragments of the Escherichia coli DNA gyrase A protein
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46
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The C-terminal domain of the Escherichia coli DNA gyrase A subunit is a DNA-binding protein
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Nucleic Acids Res
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Reece1
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48
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0028294213
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Three-dimensional model of Escherichia coli DNA gyrase B subunit crystallized in two-dimensions on novobiocin-linked phospholipid films
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of special interest, Three-dimensional electron microscopy reconstruction of the structure of the intact B-subunit of DNA gyrase. A two-dimensional array of protein was created on a novobiocin-linked phospholipid film and studied by electron microscopy of negatively stained samples to 25Åand also in projection to 10Åby cryomicroscopy. The reconstruction shows that the protein has a ‘V’ shape, with the arms of the V pointing away from the novobiocin-binding site. The 43 kDa fragment of gyrase, whose crystallographic structure is known, was located at the bottom of one of the arms of the V, suggesting that the novobiocin-binding site may be close to the ATP-binding site.
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J Mol Biol
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Celia1
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Two-dimensional crystallization technique for imaging macromolecules, with application to antigen-antibody complement complexes
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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
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