2Q2E

Crystal structure of the topoisomerase VI holoenzyme from Methanosarcina mazei

2Q2E の概要

• エントリーDOI: 10.2210/pdb2q2e/pdb
• 分子名称: Type II DNA topoisomerase VI subunit A, Type 2 DNA topoisomerase 6 subunit B (2 entities in total)
• 機能のキーワード: topoisomerase, dna-binding, spo11, atpase, isomerase
• 由来する生物種: Methanosarcina mazei; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 111032.66

構造登録者

Corbett, K.D.,Benedetti, P.,Berger, J.M. (登録日: 2007-05-28, 公開日: 2007-07-10, 最終更新日: 2024-02-21)

主引用文献

Corbett, K.D.,Benedetti, P.,Berger, J.M.
Holoenzyme assembly and ATP-mediated conformational dynamics of topoisomerase VI
Nat.Struct.Mol.Biol., 14:611-619, 2007

PubMed Abstract: Type II topoisomerases help disentangle chromosomes to facilitate cell division. To advance understanding of the structure and dynamics of these essential enzymes, we have determined the crystal structure of an archaeal type IIB topoisomerase, topo VI, at 4.0-A resolution. The 220-kDa heterotetramer adopts a 'twin-gate' architecture, in which a pair of ATPase domains at one end of the enzyme is poised to coordinate DNA movements into the enzyme and through a set of DNA-cleaving domains at the other end. Small-angle X-ray scattering studies show that nucleotide binding elicits a major structural reorganization that is propagated to the enzyme's DNA-cleavage center, explaining how ATP is coupled to DNA capture and strand scission. These data afford important insights into the mechanisms of topo VI and related proteins, including type IIA topoisomerases and the Spo11 meiotic recombination endonuclease.

PubMed: 17603498
DOI: 10.1038/nsmb1264

実験手法

X-RAY DIFFRACTION (4 Å)