4LZB

Uracil binding pocket in Vaccinia virus uracil DNA glycosylase

4LZB の概要

• エントリーDOI: 10.2210/pdb4lzb/pdb
• 関連するPDBエントリー: 4DOF
• 分子名称: Uracil-DNA glycosylase, DIMETHYL SULFOXIDE, POTASSIUM ION, ... (7 entities in total)
• 機能のキーワード: alpha/beta dna glycosylase fold, viral processivity factor, dna binding component, dna repair, a20, hydrolase
• 由来する生物種: Vaccinia virus (VACV)
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 331044.21

構造登録者

Schormann, N.,Chattopadhyay, D. (登録日: 2013-07-31, 公開日: 2013-12-11, 最終更新日: 2023-09-20)

主引用文献

Schormann, N.,Banerjee, S.,Ricciardi, R.,Chattopadhyay, D.
Structure of the uracil complex of Vaccinia virus uracil DNA glycosylase.
Acta Crystallogr.,Sect.F, 69:1328-1334, 2013

PubMed Abstract: Poxvirus uracil DNA glycosylases are the most diverse members of the family I uracil DNA glycosylases (UNGs). The crystal structure of the uracil complex of Vaccinia virus uracil DNA glycosylase (D4) was determined at 2.03 Å resolution. One uracil molecule was located in the active-site pocket in each of the 12 noncrystallographic symmetry-related D4 subunits. Although the UNGs of the poxviruses (including D4) feature significant differences in the characteristic motifs designated for uracil recognition and in the base-excision mechanism, the architecture of the active-site pocket in D4 is very similar to that in UNGs of other organisms. Overall, the interactions of the bound uracil with the active-site residues are also similar to the interactions previously observed in the structures of human and Escherichia coli UNG.

PubMed: 24316823
DOI: 10.1107/S1744309113030613

実験手法

X-RAY DIFFRACTION (2.03 Å)