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PDBsum entry 1tau
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Transferase/DNA
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PDB id
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1tau
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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 taq polymerase with DNA at the polymerase active site.
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Authors
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S.H.Eom,
J.Wang,
T.A.Steitz.
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Ref.
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Nature, 1996,
382,
278-281.
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PubMed id
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Abstract
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The DNA polymerase from Thermus aquaticus (Taq polymerase) is homologous to
Escherichia coli DNA polymerase I (Pol I) and likewise has domains responsible
for DNA polymerase and 5' nuclease activities. The structures to the polymerase
domains of Taq polymerase and of the Klenow fragment (KF) of Pol I are almost
identical, whereas the structure of a vestigial editing 3'-5' exonuclease domain
of Taq polymerase that lies between the other two domains is dramatically
altered, resulting in the absence of this activity in the thermostable enzyme.
The structures have been solved for editing complexes between KF and
single-stranded DNA and for duplex DNA with a 3' overhanging single strand, but
not for a complex containing duplex DNA at the polymerase active-site. Here we
present the co-crystal structure of Taq polymerase with a blunt-ended duplex DNA
bound to the polymerase active-site cleft; the DNA neither bends nor goes
through the large polymerase cleft, and the structural form of the bound DNA is
between the B and A forms. A wide minor groove allows access to protein side
chains that hydrogen-bond to the N3 of purines and the O2 of pyrimidines at the
blunt-end terminus. Part of the DNA bound to the polymerase site shares a common
binding site with DNA bound to the exonuclease site, but they are translated
relative to each other by several angstroms along their helix axes.
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Secondary reference #1
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Title
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Crystal structure of thermus aquaticus DNA polymerase.
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Authors
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Y.Kim,
S.H.Eom,
J.Wang,
D.S.Lee,
S.W.Suh,
T.A.Steitz.
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Ref.
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Nature, 1995,
376,
612-616.
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PubMed id
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Secondary reference #2
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Title
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Isolation, Characterization, And expression in escherichia coli of the DNA polymerase gene from thermus aquaticus.
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Authors
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F.C.Lawyer,
S.Stoffel,
R.K.Saiki,
K.Myambo,
R.Drummond,
D.H.Gelfand.
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Ref.
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J Biol Chem, 1989,
264,
6427-6437.
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PubMed id
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