1LAU
URACIL-DNA GLYCOSYLASE
1LAU の概要
| エントリーDOI | 10.2210/pdb1lau/pdb |
| 分子名称 | DNA (5'-D(*TP*TP*T)-3'), PROTEIN (URACIL-DNA GLYCOSYLASE (E.C.3.2.2.-)) (3 entities in total) |
| 機能のキーワード | hydrolase, glycosidase, dna, hydrolase-dna complex, hydrolase/dna |
| 由来する生物種 | Human herpesvirus 1 (Herpes simplex virus type 1) |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 28234.07 |
| 構造登録者 | |
| 主引用文献 | Savva, R.,McAuley-Hecht, K.,Brown, T.,Pearl, L. The structural basis of specific base-excision repair by uracil-DNA glycosylase. Nature, 373:487-493, 1995 Cited by PubMed Abstract: The 1.75-A crystal structure of the uracil-DNA glycosylase from herpes simplex virus type-1 reveals a new fold, distantly related to dinucleotide-binding proteins. Complexes with a trideoxynucleotide, and with uracil, define the DNA-binding site and allow a detailed understanding of the exquisitely specific recognition of uracil in DNA. The overall structure suggests binding models for elongated single- and double-stranded DNA substrates. Conserved residues close to the uracil-binding site suggest a catalytic mechanism for hydrolytic base excision. PubMed: 7845459DOI: 10.1038/373487a0 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.8 Å) |
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