6QPQ

The structure of the cohesin head module elucidates the mechanism of ring opening

6QPQ の概要

• エントリーDOI: 10.2210/pdb6qpq/pdb
• 分子名称: Structural maintenance of chromosomes protein,Structural maintenance of chromosomes protein, Sister chromatid cohesion protein 1 (3 entities in total)
• 機能のキーワード: cohesin, cell division, genome regulation, sister chromatid cohesion, smc, kleisin, cell cycle
• 由来する生物種: Chaetomium thermophilum var. thermophilum DSM 1495; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 230471.83

構造登録者

Li, Y.,Muir, K.W.,Panne, D. (登録日: 2019-02-14, 公開日: 2020-02-05, 最終更新日: 2024-05-15)

主引用文献

Muir, K.W.,Li, Y.,Weis, F.,Panne, D.
The structure of the cohesin ATPase elucidates the mechanism of SMC-kleisin ring opening.
Nat.Struct.Mol.Biol., 27:233-239, 2020

PubMed Abstract: Genome regulation requires control of chromosome organization by SMC-kleisin complexes. The cohesin complex contains the Smc1 and Smc3 subunits that associate with the kleisin Scc1 to form a ring-shaped complex that can topologically engage chromatin to regulate chromatin structure. Release from chromatin involves opening of the ring at the Smc3-Scc1 interface in a reaction that is controlled by acetylation and engagement of the Smc ATPase head domains. To understand the underlying molecular mechanisms, we have determined the 3.2-Å resolution cryo-electron microscopy structure of the ATPγS-bound, heterotrimeric cohesin ATPase head module and the 2.1-Å resolution crystal structure of a nucleotide-free Smc1-Scc1 subcomplex from Saccharomyces cerevisiae and Chaetomium thermophilium. We found that ATP-binding and Smc1-Smc3 heterodimerization promote conformational changes within the ATPase that are transmitted to the Smc coiled-coil domains. Remodeling of the coiled-coil domain of Smc3 abrogates the binding surface for Scc1, thus leading to ring opening at the Smc3-Scc1 interface.

PubMed: 32066964
DOI: 10.1038/s41594-020-0379-7

実験手法

X-RAY DIFFRACTION (2.1 Å)