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PDBsum entry 1kln
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Transferase/DNA
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PDB id
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1kln
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structure of DNA polymerase I klenow fragment bound to duplex DNA.
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Authors
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L.S.Beese,
V.Derbyshire,
T.A.Steitz.
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Ref.
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Science, 1993,
260,
352-355.
[DOI no: ]
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PubMed id
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Abstract
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Klenow fragment of Escherichia coli DNA polymerase I, which was cocrystallized
with duplex DNA, positioned 11 base pairs of DNA in a groove that lies at right
angles to the cleft that contains the polymerase active site and is adjacent to
the 3' to 5' exonuclease domain. When the fragment bound DNA, a region
previously referred to as the "disordered domain" became more ordered
and moved along with two helices toward the 3' to 5' exonuclease domain to form
the binding groove. A single-stranded, 3' extension of three nucleotides bound
to the 3' to 5' exonuclease active site. Although this cocrystal structure
appears to be an editing complex, it suggests that the primer strand approaches
the catalytic site of the polymerase from the direction of the 3' to 5'
exonuclease domain and that the duplex DNA product may bend to enter the cleft
that contains the polymerase catalytic site.
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Secondary reference #1
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Title
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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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Authors
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L.S.Beese,
T.A.Steitz.
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Ref.
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Embo J, 1991,
10,
25-33.
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PubMed id
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Secondary reference #2
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Title
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Cocrystal structure of an editing complex of klenow fragment with DNA.
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Authors
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P.S.Freemont,
J.M.Friedman,
L.S.Beese,
M.R.Sanderson,
T.A.Steitz.
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Ref.
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Proc Natl Acad Sci U S A, 1988,
85,
8924-8928.
[DOI no: ]
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PubMed id
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Secondary reference #3
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Title
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Structure of large fragment of escherichia coli DNA polymerase i complexed with dtmp.
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Authors
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D.L.Ollis,
P.Brick,
R.Hamlin,
N.G.Xuong,
T.A.Steitz.
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Ref.
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Nature, 1985,
313,
762-766.
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PubMed id
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