2CSB

Crystal structure of Topoisomerase V from Methanopyrus kandleri (61 kDa fragment)

2CSB の概要

• エントリーDOI: 10.2210/pdb2csb/pdb
• 関連するPDBエントリー: 2CSD
• 分子名称: Topoisomerase V, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: topoisomerase ib, topoisomerase v, helix-turn-helix, helix-hairpin-helix, hhh motif, three helix bundle, methanopyrus kandleri, 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: 120686.88

構造登録者

Taneja, B.,Patel, A.,Slesarev, A.,Mondragon, A. (登録日: 2005-05-21, 公開日: 2006-01-31, 最終更新日: 2024-11-20)

主引用文献

Taneja, B.,Patel, A.,Slesarev, A.,Mondragon, A.
Structure of the N-terminal fragment of topoisomerase V reveals a new family of topoisomerases
Embo J., 25:398-408, 2006

PubMed Abstract: Topoisomerases are involved in controlling and maintaining the topology of DNA and are present in all kingdoms of life. Unlike all other types of topoisomerases, similar type IB enzymes have only been identified in bacteria and eukarya. The only putative type IB topoisomerase in archaea is represented by Methanopyrus kandleri topoisomerase V. Despite several common functional characteristics, topoisomerase V shows no sequence similarity to other members of the same type. The structure of the 61 kDa N-terminal fragment of topoisomerase V reveals no structural similarity to other topoisomerases. Furthermore, the structure of the active site region is different, suggesting no conservation in the cleavage and religation mechanism. Additionally, the active site is buried, indicating the need of a conformational change for activity. The presence of a topoisomerase in archaea with a unique structure suggests the evolution of a separate mechanism to alter DNA.

PubMed: 16395333
DOI: 10.1038/sj.emboj.7600922

実験手法

X-RAY DIFFRACTION (2.3 Å)