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Volumn 7, Issue 1, 1997, Pages 103-109

DNA-repair enzymes

Author keywords

[No Author keywords available]

Indexed keywords

ENDONUCLEASE; POLYDEOXYRIBONUCLEOTIDE SYNTHASE;

EID: 0031056091     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(97)80013-9     Document Type: Article
Times cited : (29)

References (49)
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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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    • 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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    • 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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    • 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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    • 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.
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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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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.