4QCB
Protein-DNA complex of Vaccinia virus D4 with double-stranded non-specific DNA
4QCB の概要
| エントリーDOI | 10.2210/pdb4qcb/pdb |
| 関連するPDBエントリー | 4DOF 4DOG 4LZB 4QC9 4QCA |
| 分子名称 | Uracil-DNA glycosylase, 5'-D(*GP*CP*AP*AP*AP*CP*GP*TP*TP*TP*GP*C)-3', GLYCEROL, ... (4 entities in total) |
| 機能のキーワード | dna repair enzyme, component of processivity factor, a20, poxvirus, hydrolase-dna complex, hydrolase/dna |
| 由来する生物種 | Vaccinia virus (VACV) |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 58421.24 |
| 構造登録者 | Schormann, N.,Banerjee, S.,Ricciardi, R.,Chattopadhyay, D. (登録日: 2014-05-09, 公開日: 2015-06-10, 最終更新日: 2023-09-20) |
| 主引用文献 | Schormann, N.,Banerjee, S.,Ricciardi, R.,Chattopadhyay, D. Binding of undamaged double stranded DNA to vaccinia virus uracil-DNA Glycosylase. BMC Struct. Biol., 15:10-10, 2015 Cited by PubMed Abstract: Uracil-DNA glycosylases are evolutionarily conserved DNA repair enzymes. However, vaccinia virus uracil-DNA glycosylase (known as D4), also serves as an intrinsic and essential component of the processive DNA polymerase complex during DNA replication. In this complex D4 binds to a unique poxvirus specific protein A20 which tethers it to the DNA polymerase. At the replication fork the DNA scanning and repair function of D4 is coupled with DNA replication. So far, DNA-binding to D4 has not been structurally characterized. PubMed: 26031450DOI: 10.1186/s12900-015-0037-1 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.89 Å) |
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