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Hatahet Z, Kow YW, Purmal AA, Cunningham RP, Wallace SS. New substrates for old enzymes, 5-hydroxy-2'-deoxycytidine and 5-hydroxy-2'-deoxyuridine are substrates for Escherichia coli endonuclease III and formamidopyrimidine DNA N-glycosylase, while 5-hydroxy-2'-deoxyuridine is a substrate for uracil DNA N-glycosylase. J Biol Chem. 269:1994;18814-18820.
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of outstanding interest. On the basis of the high-resolution crystal structure and a mutational analysis of the enzyme, the authors propose a structural basis for endo III - DNA binding and catalysis, involving two novel HhH and FCL DNA-binding motifs.
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Thayer MM, Ahern H, Xing D, Cunningham RP, Tainer JA. Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure. of outstanding interest EMBO J. 14:1995;4108-4120 On the basis of the high-resolution crystal structure and a mutational analysis of the enzyme, the authors propose a structural basis for endo III - DNA binding and catalysis, involving two novel HhH and FCL DNA-binding motifs.
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24
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Bjelland S, Birkeland N-K, Benneche T, Volden G, Seeberg E. DNA glycosylase activities for thymine residues oxidized in the methyl group are functions of AlkA in Escherichia coli. J Biol Chem. 269:1994;30489-30495.
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Saparbaev M, Laval J. Excision of hypoxanthine from DNA containing dIMP residues by the Escherichia coli, yeast, rat and human alkylpurine DNA glycosylases. Proc Natl Acad Sci USA. 91:1994;5873-5877.
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of outstanding interest. The structural analysis of AlkA at 2.3 Å resolution reveal that the 3D structures of the DNA-binding and catalytic domains are similar to those of two domains of endo III. The major catalytic residue, Asp238, determined by mutational analysis, is located in the cavity on the interface between the two domains. A tentative model of the enzyme - DNA complex is proposed.
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Yamagata Y, Kato M, Odawara K, Tokuno Y, Nakashima Y, Matsushima N, Yasumura K, Tomita K, Ihara K, Fujii Y, et al. Three-dimensional structure of a DNA repair enzyme, 3-methyladenine DNA glycosylase II, from Escherichia coli. of outstanding interest Cell. 86:1996;311-319 The structural analysis of AlkA at 2.3 Å resolution reveal that the 3D structures of the DNA-binding and catalytic domains are similar to those of two domains of endo III. The major catalytic residue, Asp238, determined by mutational analysis, is located in the cavity on the interface between the two domains. A tentative model of the enzyme - DNA complex is proposed.
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Yamagata, Y.1
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of outstanding interest. The crystal structure of the DNA repair enzyme AlkA refined to 1.8 Å resolution is presented. The significance of Asp238 in catalysis was confirmed by mutagenesis studies. The binding site for the alkylated bases is proposed to reside in a large hydrophobic cleft that is mostly occupied by aromatic residues.
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Labahn J, Scharer OD, Long A, Ezaz-Nikpay K, Verdine GL, Ellenberger TE. Structural basis for the excision repair of alkylation-damaged DNA. of outstanding interest Cell. 86:1996;321-329 The crystal structure of the DNA repair enzyme AlkA refined to 1.8 Å resolution is presented. The significance of Asp238 in catalysis was confirmed by mutagenesis studies. The binding site for the alkylated bases is proposed to reside in a large hydrophobic cleft that is mostly occupied by aromatic residues.
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Labahn, J.1
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Michaels ML, Tchou J, Grollman AP, Miller JH. A repair system for 8-oxo-7,8-dihydrodeoxyguanine. Biochemistry. 31:1992;10964-10968.
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Escherichia coli MutY protein has both N-glycosylase and apurinic/apyrimidinic endonuclease activities on C and A-G mispairs
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Tsai-Wu J-J, Liu H-F, Lu A-L. Escherichia coli MutY protein has both N-glycosylase and apurinic/apyrimidinic endonuclease activities on C and A-G mispairs. Proc Natl Acad Sci USA. 89:1992;8779-8783.
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Purification of a mammalian homologue of Escherichia coli endonuclease III: Identification of a bovine pyrimidine hydrate-thymine glycol DNA-glycosylase/AP lyase by irreversible cross linking to a thymine glycol-containing oligodeoxynucleotide
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Hilbert P, Boorstein RJ, Kung HC, Bolton PH, Xing D, Cunningham RP, Teebor GW. Purification of a mammalian homologue of Escherichia coli endonuclease III: identification of a bovine pyrimidine hydrate-thymine glycol DNA-glycosylase/AP lyase by irreversible cross linking to a thymine glycol-containing oligodeoxynucleotide. Biochemistry. 35:1996;2505-2511.
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Hilbert, P.1
Boorstein, R.J.2
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Cloning of a yeast 8-oxoguanine DNA glycosylase reveals the existence of a base-excision DNA-repair protein superfamily
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of special interest. The yeast DNA glycosylase (Ogg1) specific to 8-oxoguanine is suggested to be closely related in 3D structure to endo III. The sequence motif shared between Ogg1, endo III, and AlkA was found in a number of other enzymes. This finding led to the proposal of a structural superfamily of DNA repair enzymes.
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Nash HM, Bruner SD, Scharer OD, Kawate T, Addona TA, Spooner E, Lane WS, Verdine GL. Cloning of a yeast 8-oxoguanine DNA glycosylase reveals the existence of a base-excision DNA-repair protein superfamily. of special interest Curr Biol. 6:1996;968-980 The yeast DNA glycosylase (Ogg1) specific to 8-oxoguanine is suggested to be closely related in 3D structure to endo III. The sequence motif shared between Ogg1, endo III, and AlkA was found in a number of other enzymes. This finding led to the proposal of a structural superfamily of DNA repair enzymes.
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Curr Biol
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Nash, H.M.1
Bruner, S.D.2
Scharer, O.D.3
Kawate, T.4
Addona, T.A.5
Spooner, E.6
Lane, W.S.7
Verdine, G.L.8
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35
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0028933306
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Properties of recombinant human uracil-DNA glycosylase from the UNG-gene and evidence that UNG-gene encodes the major uracil-DNA glycosylase
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Slupphaug G, Eftedal I, Kavli B, Bharati S, Helle NM, Haug T, Levine DW, Krokan HE. Properties of recombinant human uracil-DNA glycosylase from the UNG-gene and evidence that UNG-gene encodes the major uracil-DNA glycosylase. Biochemistry. 34:1995;128-138.
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Biochemistry
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Slupphaug, G.1
Eftedal, I.2
Kavli, B.3
Bharati, S.4
Helle, N.M.5
Haug, T.6
Levine, D.W.7
Krokan, H.E.8
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36
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0028959237
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The structural basis of specific base-excision repair by uracil-DNA glycosylase
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of special interest. The high-resolution crystal structures of UDG from herpes simplex virus, both in its free form and in complexes with a trinucleotide and uracil, reveal a new protein fold and allow the authors to propose mechanisms of DNA binding and catalysis.
-
Savva R, McAuley-Hecht K, Brown T, Pearl L. The structural basis of specific base-excision repair by uracil-DNA glycosylase. of special interest Nature. 373:1995;487-493 The high-resolution crystal structures of UDG from herpes simplex virus, both in its free form and in complexes with a trinucleotide and uracil, reveal a new protein fold and allow the authors to propose mechanisms of DNA binding and catalysis.
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Nature
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Savva, R.1
McAuley-Hecht, K.2
Brown, T.3
Pearl, L.4
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37
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Crystal structure and mutational analysis of human uracil-DNA glycosylase: Structural basis for specificity and catalysis
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of special interest. The crystal structures of the free form of glycosylase and its complex with 6-aminouracil, in combination with a mutational analysis, reveal the uracil-binding site, the catalytic residues, and the positively charged groove that is involved in DNA binding. The mechanism of the catalytic reaction is proposed.
-
Mol CD, Arvai AS, Slupphaug G, Kavli B, Alseth I, Krokan HE, Tainer JA. Crystal structure and mutational analysis of human uracil-DNA glycosylase: structural basis for specificity and catalysis. of special interest Cell. 80:1995;869-878 The crystal structures of the free form of glycosylase and its complex with 6-aminouracil, in combination with a mutational analysis, reveal the uracil-binding site, the catalytic residues, and the positively charged groove that is involved in DNA binding. The mechanism of the catalytic reaction is proposed.
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Cell
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, pp. 869-878
-
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Mol, C.D.1
Arvai, A.S.2
Slupphaug, G.3
Kavli, B.4
Alseth, I.5
Krokan, H.E.6
Tainer, J.A.7
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38
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0029084487
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Crystal structure of human uracil-DNA glycosylase in complex with a protein inhibitor: Protein mimicry of DNA
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of special interest. The atomic structure of the complex of hUDG with a protein inhibitor, UGI, has been refined to 1.9 Å resolution. UGI was shown to bind to the DNA-binding loop of the hUDG, and to form no contacts with the uracil-binding pocket. A specific role in DNA binding is proposed for Leu272 of UDG.
-
Mol CD, Arvai AS, Sanderson RJ, Slupphaug G, Kavli B, Mosbaugh DW, Krokan HE, Tainer JA. Crystal structure of human uracil-DNA glycosylase in complex with a protein inhibitor: protein mimicry of DNA. of special interest Cell. 82:1995;701-708 The atomic structure of the complex of hUDG with a protein inhibitor, UGI, has been refined to 1.9 Å resolution. UGI was shown to bind to the DNA-binding loop of the hUDG, and to form no contacts with the uracil-binding pocket. A specific role in DNA binding is proposed for Leu272 of UDG.
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Cell
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Mol, C.D.1
Arvai, A.S.2
Sanderson, R.J.3
Slupphaug, G.4
Kavli, B.5
Mosbaugh, D.W.6
Krokan, H.E.7
Tainer, J.A.8
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39
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0029115366
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Nucleotide mimicry in the crystal structure of the uracil-DNA glycosylase-uracil glycosylase inhibitor protein complex
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of special interest. The crystal structure of HSV-1UDG in complex with a protein inhibitor (UGI) shows that UGI directly mimics the enzyme - DNA interactions observed in the HSV-1UDG - trinucleotide complex. UGI is shown to block access to the active site of the enzyme but to form no contacts within the uracil-binding pocket.
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Savva R, Pearl L. Nucleotide mimicry in the crystal structure of the uracil-DNA glycosylase-uracil glycosylase inhibitor protein complex. of special interest Nat Struct Biol. 373:1995;752-757 The crystal structure of HSV-1UDG in complex with a protein inhibitor (UGI) shows that UGI directly mimics the enzyme - DNA interactions observed in the HSV-1UDG - trinucleotide complex. UGI is shown to block access to the active site of the enzyme but to form no contacts within the uracil-binding pocket.
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Nat Struct Biol
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Savva, R.1
Pearl, L.2
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40
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0029904839
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Structure of human uracil-DNA glycosylase bound to DNA shows a nucleotide flipping mechanism
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of outstanding interest. The structure of hUDG(Leu272→Arg/Asp 145→Asn) - DNA directly reveals the DNA - binding mechanism of hUDG and its cognate DNA substrate. The mutation Leu272→Arg abolishes the release of the product DNA from the protein but does not affect the glycosylase activity of the enzyme, so that the uracil in the complex is cleaved from the sugar moiety.
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Slupphaug G, Mol CD, Kavli B, Arvai AS, Krokan HE, Tainer JA. Structure of human uracil-DNA glycosylase bound to DNA shows a nucleotide flipping mechanism. of outstanding interest Nature. 384:1996;87-92 The structure of hUDG(Leu272→Arg/Asp 145→Asn) - DNA directly reveals the DNA - binding mechanism of hUDG and its cognate DNA substrate. The mutation Leu272→Arg abolishes the release of the product DNA from the protein but does not affect the glycosylase activity of the enzyme, so that the uracil in the complex is cleaved from the sugar moiety.
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Nature
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Slupphaug, G.1
Mol, C.D.2
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