4UVK

Cohesin subunit Scc3 from Z. rouxii, 88-1035

4UVK の概要

• エントリーDOI: 10.2210/pdb4uvk/pdb
• 関連するPDBエントリー: 4UVJ
• 分子名称: ZYRO0D15994P (2 entities in total)
• 機能のキーワード: cell cycle, cohesin, mitosis, heat repeats, smc proteins
• 由来する生物種: ZYGOSACCHAROMYCES ROUXII
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 109749.08

構造登録者

Roig, M.B.,Nasmyth, K.,Lowe, J. (登録日: 2014-08-06, 公開日: 2014-08-20, 最終更新日: 2024-05-08)

主引用文献

Roig, M.B.,Lowe, J.,Chan, K.L.,Beckouet, F.,Metson, J.,Nasmyth, K.
Structure and Function of Cohesins Scc3/Sa Regulatory Subunit
FEBS Lett., 588:3692-, 2014

PubMed Abstract: Sister chromatid cohesion involves entrapment of sister DNAs by a cohesin ring created through association of a kleisin subunit (Scc1) with ATPase heads of Smc1/Smc3 heterodimers. Cohesin's association with chromatin involves subunits recruited by Scc1: Wapl, Pds5, and Scc3/SA, in addition to Scc2/4 loading complex. Unlike Pds5, Wapl, and Scc2/4, Scc3s are encoded by all eukaryotic genomes. Here, a crystal structure of Scc3 reveals a hook-shaped protein composed of tandem α helices. Its N-terminal domain contains a conserved and essential surface (CES) present even in organisms lacking Pds5, Wapl, and Scc2/4, while its C-terminal domain binds a section of the kleisin Scc1. Scc3 turns over in G2/M while maintaining cohesin's association with chromosomes and it promotes de-acetylation of Smc3 upon Scc1 cleavage.

PubMed: 25171859
DOI: 10.1016/J.FEBSLET.2014.08.015

実験手法

X-RAY DIFFRACTION (2.6 Å)