1Z5A

Topoisomerase VI-B, ADP-bound dimer form

1Z5A の概要

• エントリーDOI: 10.2210/pdb1z5a/pdb
• 関連するPDBエントリー: 1MU5 1MX0 1Z59 1Z5B 1Z5C
• 分子名称: Type II DNA topoisomerase VI subunit B, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: topoisomerase, archaea, atpase, isomerase
• 由来する生物種: Sulfolobus shibatae
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 107923.74

構造登録者

Corbett, K.D.,Berger, J.M. (登録日: 2005-03-17, 公開日: 2005-06-14, 最終更新日: 2023-08-23)

主引用文献

Corbett, K.D.,Berger, J.M.
Structural dissection of ATP turnover in the prototypical GHL ATPase TopoVI.
Structure, 13:873-882, 2005

PubMed Abstract: GHL proteins are functionally diverse enzymes defined by the presence of a conserved ATPase domain that self-associates to trap substrate upon nucleotide binding. The structural states adopted by these enzymes during nucleotide hydrolysis and product release, and their consequences for enzyme catalysis, have remained unclear. Here, we have determined a complete structural map of the ATP turnover cycle for topoVI-B, the ATPase subunit of the archaeal GHL enzyme topoisomerase VI. With this ensemble of structures, we show that significant conformational changes in the subunit occur first upon ATP binding, and subsequently upon release of hydrolyzed P(i). Together, these data provide a structural framework for understanding the role of ATP hydrolysis in the type II topoisomerase reaction. Our results also suggest that the GHL ATPase module is a molecular switch in which ATP hydrolysis serves as a prerequisite but not a driving force for substrate-dependent structural transitions in the enzyme.

PubMed: 15939019
DOI: 10.1016/j.str.2005.03.013

実験手法

X-RAY DIFFRACTION (2.2 Å)