8ROG

Human cohesin SMC1A-HD(shortCC-EQ)/RAD21-C complex - ATPgS-Mg-bound conformation

8ROG の概要

• エントリーDOI: 10.2210/pdb8rog/pdb
• 分子名称: Structural maintenance of chromosomes protein 1A, 64-kDa C-terminal product, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: 3d genome organization, chromatin, cohesin, atpase activity, atpase cycle, nuclear protein
• 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: 50416.33

構造登録者

Vitoria Gomes, M.,Romier, C. (登録日: 2024-01-11, 公開日: 2024-09-11, 最終更新日: 2024-09-18)

主引用文献

Vitoria Gomes, M.,Landwerlin, P.,Diebold-Durand, M.L.,Shaik, T.B.,Durand, A.,Troesch, E.,Weber, C.,Brillet, K.,Lemee, M.V.,Decroos, C.,Dulac, L.,Antony, P.,Watrin, E.,Ennifar, E.,Golzio, C.,Romier, C.
The cohesin ATPase cycle is mediated by specific conformational dynamics and interface plasticity of SMC1A and SMC3 ATPase domains.
Cell Rep, 43:114656-114656, 2024

PubMed Abstract: Cohesin is key to eukaryotic genome organization and acts throughout the cell cycle in an ATP-dependent manner. The mechanisms underlying cohesin ATPase activity are poorly understood. Here, we characterize distinct steps of the human cohesin ATPase cycle and show that the SMC1A and SMC3 ATPase domains undergo specific but concerted structural rearrangements along this cycle. Specifically, whereas the proximal coiled coil of the SMC1A ATPase domain remains conformationally stable, that of the SMC3 displays an intrinsic flexibility. The ATP-dependent formation of the heterodimeric SMC1A/SMC3 ATPase module (engaged state) favors this flexibility, which is counteracted by NIPBL and DNA binding (clamped state). Opening of the SMC3/RAD21 interface (open-engaged state) stiffens the SMC3 proximal coiled coil, thus constricting together with that of SMC1A the ATPase module DNA-binding chamber. The plasticity of the ATP-dependent interface between the SMC1A and SMC3 ATPase domains enables these structural rearrangements while keeping the ATP gate shut. VIDEO ABSTRACT.

PubMed: 39240714
DOI: 10.1016/j.celrep.2024.114656

実験手法

X-RAY DIFFRACTION (1.94 Å)