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1
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0031587827
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Crystal structure of a pol α replication DNA polymerase from bacteriophage RB69
-
of outstanding interest. The authors describe the first crystal structure of either a pol α or 'B family' polymerase. This structure has wide-ranging implications for the relatedness of DNA polymerases, proof-reading, the organization of the RB69 replisome and eukaryotic DNA polymerases that could not be modeled on the pol I enzyme.
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of outstanding interest Wang J, Sattar AKMA, Wang CC, Karam JD, Konigsberg WH, Steitz TA. Crystal structure of a pol α replication DNA polymerase from bacteriophage RB69. Cell. 89:1997;1087-1089 The authors describe the first crystal structure of either a pol α or 'B family' polymerase. This structure has wide-ranging implications for the relatedness of DNA polymerases, proof-reading, the organization of the RB69 replisome and eukaryotic DNA polymerases that could not be modeled on the pol I enzyme.
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Cell
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Wang, J.1
Sattar, A.K.M.A.2
Wang, C.C.3
Karam, J.D.4
Konigsberg, W.H.5
Steitz, T.A.6
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2
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0032518398
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Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution
-
of outstanding interest. The elucidation of the structure of the ternary complex of T7 DNA polymerase with its substrates is described. This 2.2 Å resolution structure shows how substrates bind to this KF-like polymerase and suggests a mechanism by which thioredoxin allows the DNA to stay associated with the polymerase. A detailed view of the active site shows that the catalytic mechanism involves two metal ions.
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of outstanding interest Doublié S, Tabor S, Long AM, Richardson CC, Ellenberger T. Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution. Nature. 391:1998;251-258 The elucidation of the structure of the ternary complex of T7 DNA polymerase with its substrates is described. This 2.2 Å resolution structure shows how substrates bind to this KF-like polymerase and suggests a mechanism by which thioredoxin allows the DNA to stay associated with the polymerase. A detailed view of the active site shows that the catalytic mechanism involves two metal ions.
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Nature
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Doublié, S.1
Tabor, S.2
Long, A.M.3
Richardson, C.C.4
Ellenberger, T.5
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3
-
-
0031568308
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Crystal structure of a thermostable Bacillus DNA polymerase I large fragment at 2.1 Å resolution
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of special interest. The high-resolution structure of the large fragment of this enzyme shows that the polymerase domain of pol I from B. stearothermophilus is shown to be highly homologous to the same domain of KF. The structural basis for the lack of 3′-5′ exonuclease activity of the Bacillus enzyme is also discussed.
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of special interest Kiefer JR, Mao C, Hansen CJ, Basehore SL, Hogrefe HH, Braman JC, Beese LS. Crystal structure of a thermostable Bacillus DNA polymerase I large fragment at 2.1 Å resolution. Structure. 5:1997;95-108 The high-resolution structure of the large fragment of this enzyme shows that the polymerase domain of pol I from B. stearothermophilus is shown to be highly homologous to the same domain of KF. The structural basis for the lack of 3′-5′ exonuclease activity of the Bacillus enzyme is also discussed.
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Structure
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Kiefer, J.R.1
Mao, C.2
Hansen, C.J.3
Basehore, S.L.4
Hogrefe, H.H.5
Braman, J.C.6
Beese, L.S.7
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4
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0030592095
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Structure of Taq polymerase with DNA at the polymerase active site
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of outstanding interest. The structure of a binary complex of Taq pol and blunt-ended DNA shows that the DNA binds with the blunt end stacked against the fingers and the double-stranded portion leaving the active site between the thumb and the vestigial exonuclease domain.
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of outstanding interest Eom SH, Wang J, Steitz TA. Structure of Taq polymerase with DNA at the polymerase active site. Nature. 382:1996;278-281 The structure of a binary complex of Taq pol and blunt-ended DNA shows that the DNA binds with the blunt end stacked against the fingers and the double-stranded portion leaving the active site between the thumb and the vestigial exonuclease domain.
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Nature
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Eom, S.H.1
Wang, J.2
Steitz, T.A.3
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5
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0029817866
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Crystal structures of human DNA polymerase β complexed with DNA: Implications for catalytic mechanism, processivity, and fidelity
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of special interest. The authors describe several binary complexes of pol β and DNA. These complexes reveal facts about the processivity, fidelity and the conformational changes upon nucleotide binding. In addition, a model for the binding of pol β to gapped DNA is proposed and discussed in these contexts.
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of special interest Pelletier H, Sawaya MR, Wolfle W, Wilson S, Kraut J. Crystal structures of human DNA polymerase β complexed with DNA: implications for catalytic mechanism, processivity, and fidelity. Biochemistry. 35:1996;12742-12761 The authors describe several binary complexes of pol β and DNA. These complexes reveal facts about the processivity, fidelity and the conformational changes upon nucleotide binding. In addition, a model for the binding of pol β to gapped DNA is proposed and discussed in these contexts.
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Biochemistry
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Pelletier, H.1
Sawaya, M.R.2
Wolfle, W.3
Wilson, S.4
Kraut, J.5
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6
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0029784881
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A thumb subdomain mutant of the large fragment of Escherichia coli DNA polymerase I with reduced DNA binding affinity, processivity, and frameshift fidelity
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of outstanding interest. The results in this paper show that deleting 24 residues from the tip of the thumb of KF reduce the processivity of this enzyme. Further, such a polymerase mutant makes far more frameshift mutations than wild-type KF.
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of outstanding interest Minnick DT, Astatke M, Joyce CM, Kunkel TA. A thumb subdomain mutant of the large fragment of Escherichia coli DNA polymerase I with reduced DNA binding affinity, processivity, and frameshift fidelity. J Biol Chem. 271:1996;24954-24961 The results in this paper show that deleting 24 residues from the tip of the thumb of KF reduce the processivity of this enzyme. Further, such a polymerase mutant makes far more frameshift mutations than wild-type KF.
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J Biol Chem
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Minnick, D.T.1
Astatke, M.2
Joyce, C.M.3
Kunkel, T.A.4
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7
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0029843045
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A structural basis for metal ion mutagenecity and nucleotide selectivity in human DNA polymerase β
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of special interest. A variety of structures are presented that illustrate the importance of the identity of the metal ions and the base, ribose and triphosphate moieties on the binding and utilization of nucleotides by human pol β.
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of special interest Pelletier H, Sawaya MR, Wolfle W, Wilson SH, Kraut J. A structural basis for metal ion mutagenecity and nucleotide selectivity in human DNA polymerase β Biochemistry. 35:1996;12762-12777 A variety of structures are presented that illustrate the importance of the identity of the metal ions and the base, ribose and triphosphate moieties on the binding and utilization of nucleotides by human pol β.
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Biochemistry
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Pelletier, H.1
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Beese, L.S.1
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0026693137
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Kim Y, Eom SH, Wang J, Lee DS, Suh SW, Steitz TA. Crystal structure of Thermus aquaticus DNA polymerase. Nature. 376:1995;612-616.
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0029056926
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Korolev S, Nayal M, Barnes WM, DiCera E, Waksman G. Crystal structure of the large fragment of Thermus aquaticus DNA polymerase I at 2.5 Å resolution: structural basis for thermostability. Proc Natl Acad Sci USA. 92:1995;9264-9268.
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0027974928
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2.3 Å crystal structure of the catalytic domain of DNA polymerase β
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of outstanding interest. By simply grafting the thioredoxin-binding domain of T7 DNA polymerase onto the tip of the thumb of a KF, the authors show that the KF can be rendered into a thioredoxin-sensitive processive DNA polymerase. Though the overall activity of the mutant KF is lower than the wild-type, the gains in processivity are impressive.
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of outstanding interest Bedford E, Tabor S, Richardson CC. The thioredoxin binding domain of bacteriophage T7 DNA polymerase confers processivity on Escherichia coli DNA polymerase I. Proc Natl Acad Sci USA. 94:1997;479-484 By simply grafting the thioredoxin-binding domain of T7 DNA polymerase onto the tip of the thumb of a KF, the authors show that the KF can be rendered into a thioredoxin-sensitive processive DNA polymerase. Though the overall activity of the mutant KF is lower than the wild-type, the gains in processivity are impressive.
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