2H7F

Structure of variola topoisomerase covalently bound to DNA

2H7F の概要

• エントリーDOI: 10.2210/pdb2h7f/pdb
• 関連するPDBエントリー: 2H7G
• 分子名称: 5'-D(*TP*TP*GP*TP*CP*GP*CP*CP*CP*TP*T)-3', 5'-D(*TP*AP*AP*TP*AP*AP*GP*GP*GP*CP*GP*AP*CP*A)-3', DNA topoisomerase 1, ... (4 entities in total)
• 機能のキーワード: type ib topoisomerase, dna binding, protein-dna complex, isomerase, isomerase-dna complex, isomerase/dna
• 由来する生物種: Variola virus
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 44326.43

構造登録者

Perry, K.,Hwang, Y.,Bushman, F.D.,Van Duyne, G.D. (登録日: 2006-06-02, 公開日: 2006-08-15, 最終更新日: 2024-11-20)

主引用文献

Perry, K.,Hwang, Y.,Bushman, F.D.,Van Duyne, G.D.
Structural basis for specificity in the poxvirus topoisomerase.
Mol.Cell, 23:343-354, 2006

PubMed Abstract: Although smallpox has been eradicated from the human population, it is presently feared as a possible agent of bioterrorism. The smallpox virus codes for its own topoisomerase enzyme that differs from its cellular counterpart by requiring a specific DNA sequence for activation of catalysis. Here we present crystal structures of the smallpox virus topoisomerase enzyme bound both covalently and noncovalently to a specific DNA sequence. These structures reveal the basis for site-specific DNA recognition, and they explain how catalysis is likely activated by formation of a specific enzyme-DNA interface. Unexpectedly, the poxvirus enzyme uses a major groove binding alpha helix that is not present in the human enzyme to recognize part of the core recognition sequence and activate the enzyme for catalysis. The topoisomerase-DNA complex structures also provide a three-dimensional framework that may facilitate the rational design of therapeutic agents to treat poxvirus infections.

PubMed: 16885024
DOI: 10.1016/j.molcel.2006.06.015

実験手法

X-RAY DIFFRACTION (2.7 Å)