2OWQ

Crystal structure of vaccinia virus uracil-DNA glycosylase

2OWQ の概要

• エントリーDOI: 10.2210/pdb2owq/pdb
• 関連するPDBエントリー: 1AKZ 2EUG 2OWR
• 分子名称: Uracil-DNA glycosylase, CHLORIDE ION, IMIDAZOLE, ... (6 entities in total)
• 機能のキーワード: uracil-dna glycosylase fold in the core: 3 layers (a/b/a), and parallel beta-sheet of 4 strands in the order 2134; novel features: beta-sheets at n- and c-terminus, hydrolase
• 由来する生物種: Vaccinia virus Western Reserve
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 55213.38

構造登録者

Schormann, N.,Chattopadhyay, D. (登録日: 2007-02-16, 公開日: 2007-07-24, 最終更新日: 2024-02-21)

主引用文献

Schormann, N.,Grigorian, A.,Samal, A.,Krishnan, R.,DeLucas, L.,Chattopadhyay, D.
Crystal structure of vaccinia virus uracil-DNA glycosylase reveals dimeric assembly
Bmc Struct.Biol., 7:45-45, 2007

PubMed Abstract: Uracil-DNA glycosylases (UDGs) catalyze excision of uracil from DNA. Vaccinia virus, which is the prototype of poxviruses, encodes a UDG (vvUDG) that is significantly different from the UDGs of other organisms in primary, secondary and tertiary structure and characteristic motifs. It adopted a novel catalysis-independent role in DNA replication that involves interaction with a viral protein, A20, to form the processivity factor. UDG:A20 association is essential for assembling of the processive DNA polymerase complex. The structure of the protein must have provisions for such interactions with A20. This paper provides the first glimpse into the structure of a poxvirus UDG.

PubMed: 17605817
DOI: 10.1186/1472-6807-7-45

実験手法

X-RAY DIFFRACTION (2.4 Å)