3M6Z

Crystal structure of an N-terminal 44 kDa fragment of topoisomerase V in the presence of guanidium hydrochloride

3M6Z の概要

• エントリーDOI: 10.2210/pdb3m6z/pdb
• 関連するPDBエントリー: 3M6K 3M7D 3M7G
• 分子名称: Topoisomerase V, PHOSPHATE ION, MAGNESIUM ION, ... (6 entities in total)
• 機能のキーワード: helix-hairpin-helix, topoisomerase, conformational changes in protein, isomerase
• 由来する生物種: Methanopyrus kandleri
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 89449.85

構造登録者

Rajan, R.,Taneja, B.,Mondragon, A. (登録日: 2010-03-16, 公開日: 2010-08-04, 最終更新日: 2024-11-06)

主引用文献

Rajan, R.,Taneja, B.,Mondragon, A.
Structures of minimal catalytic fragments of topoisomerase v reveals conformational changes relevant for DNA binding.
Structure, 18:829-838, 2010

PubMed Abstract: Topoisomerase V is an archaeal type I topoisomerase that is unique among topoisomerases due to presence of both topoisomerase and DNA repair activities in the same protein. It is organized as an N-terminal topoisomerase domain followed by 24 tandem helix-hairpin-helix (HhH) motifs. Structural studies have shown that the active site is buried by the (HhH) motifs. Here we show that the N-terminal domain can relax DNA in the absence of any HhH motifs and that the HhH motifs are required for stable protein-DNA complex formation. Crystal structures of various topoisomerase V fragments show changes in the relative orientation of the domains mediated by a long bent linker helix, and these movements are essential for the DNA to enter the active site. Phosphate ions bound to the protein near the active site helped model DNA in the topoisomerase domain and show how topoisomerase V may interact with DNA.

PubMed: 20637419
DOI: 10.1016/j.str.2010.03.006

実験手法

X-RAY DIFFRACTION (1.4 Å)