6WG3

Cryo-EM structure of human Cohesin-NIPBL-DNA complex

6WG3 の概要

• エントリーDOI: 10.2210/pdb6wg3/pdb
• EMDBエントリー: 21658
• 分子名称: Structural maintenance of chromosomes protein 1A, Structural maintenance of chromosomes protein 3, Double-strand-break repair protein rad21 homolog, ... (8 entities in total)
• 機能のキーワード: protein-dna complex, atpase, dna-binding protein, genome organization, sister chromatid cohesion, transcription regulation, cell cycle, cell cycle-dna complex, cell cycle/dna
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 723447.98

構造登録者

Shi, Z.B.,Gao, H.,Bai, X.C.,Yu, H. (登録日: 2020-04-04, 公開日: 2020-05-20, 最終更新日: 2024-03-06)

主引用文献

Shi, Z.,Gao, H.,Bai, X.C.,Yu, H.
Cryo-EM structure of the human cohesin-NIPBL-DNA complex.
Science, 368:1454-1459, 2020

PubMed Abstract: As a ring-shaped adenosine triphosphatase (ATPase) machine, cohesin organizes the eukaryotic genome by extruding DNA loops and mediates sister chromatid cohesion by topologically entrapping DNA. How cohesin executes these fundamental DNA transactions is not understood. Using cryo-electron microscopy (cryo-EM), we determined the structure of human cohesin bound to its loader NIPBL and DNA at medium resolution. Cohesin and NIPBL interact extensively and together form a central tunnel to entrap a 72-base pair DNA. NIPBL and DNA promote the engagement of cohesin's ATPase head domains and ATP binding. The hinge domains of cohesin adopt an "open washer" conformation and dock onto the STAG1 subunit. Our structure explains the synergistic activation of cohesin by NIPBL and DNA and provides insight into DNA entrapment by cohesin.

PubMed: 32409525
DOI: 10.1126/science.abb0981

実験手法

ELECTRON MICROSCOPY (5.3 Å)