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4CHT

Crystal structure of the human topoisomerase III alpha-RMI1 complex with bound calcium ion

4CHT の概要
エントリーDOI10.2210/pdb4cht/pdb
関連するPDBエントリー4CGY
分子名称DNA TOPOISOMERASE 3-ALPHA, RECQ-MEDIATED GENOME INSTABILITY PROTEIN 1, CALCIUM ION, ... (4 entities in total)
機能のキーワードcell cycle, double holliday junction dissolution, decatenation, minimal dissolvasome
由来する生物種HOMO SAPIENS (HUMAN)
詳細
タンパク質・核酸の鎖数2
化学式量合計111326.22
構造登録者
Bocquet, N.,Bunker, R.D.,Thoma, N.H. (登録日: 2013-12-04, 公開日: 2014-02-12, 最終更新日: 2023-12-20)
主引用文献Bocquet, N.,Bizard, A.H.,Abdulrahman, W.,Larsen, N.B.,Faty, M.,Cavadini, S.,Bunker, R.D.,Kowalczykowski, S.C.,Cejka, P.,Hickson, I.D.,Thoma, N.H.
Structural and Mechanistic Insight Into Holliday-Junction Dissolution by Topoisomerase Iiialpha and Rmi1
Nat.Struct.Mol.Biol., 21:261-, 2014
Cited by
PubMed Abstract: Repair of DNA double-strand breaks via homologous recombination can produce double Holliday junctions (dHJs) that require enzymatic separation. Topoisomerase IIIα (TopIIIα) together with RMI1 disentangles the final hemicatenane intermediate obtained once dHJs have converged. How binding of RMI1 to TopIIIα influences it to behave as a hemicatenane dissolvase, rather than as an enzyme that relaxes DNA topology, is unknown. Here, we present the crystal structure of human TopIIIα complexed to the first oligonucleotide-binding domain (OB fold) of RMI1. TopIII assumes a toroidal type 1A topoisomerase fold. RMI1 attaches to the edge of the gate in TopIIIα through which DNA passes. RMI1 projects a 23-residue loop into the TopIIIα gate, thereby influencing the dynamics of its opening and closing. Our results provide a mechanistic rationale for how RMI1 stabilizes TopIIIα-gate opening to enable dissolution and illustrate how binding partners modulate topoisomerase function.
PubMed: 24509834
DOI: 10.1038/NSMB.2775
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3.25 Å)
構造検証レポート
Validation report summary of 4cht
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-01-21に公開中

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