5N22

Structure of xEco2 acetyltransferase domain bound to K106-CoA conjugate

5N22 の概要

• エントリーDOI: 10.2210/pdb5n22/pdb
• 分子名称: XEco2, GLY-ALA-LYS-LYX-ASP-GLN-TYR-PHE-LEU, (2~{S})-2-[2-[3-[[(2~{R})-4-[[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-4-oxidanyl-3-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-3,3-dimethyl-2-oxidanyl-butanoyl]amino]propanoylamino]ethylsulfanyl]propanoic acid, ... (4 entities in total)
• 機能のキーワード: cell cycle
• 由来する生物種: Xenopus laevis (African clawed frog); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 93174.47

構造登録者

Chao, W.C.H.,Wade, B.O.,Singleton, M.R. (登録日: 2017-02-07, 公開日: 2017-03-15, 最終更新日: 2024-11-06)

主引用文献

Chao, W.C.,Wade, B.O.,Bouchoux, C.,Jones, A.W.,Purkiss, A.G.,Federico, S.,O'Reilly, N.,Snijders, A.P.,Uhlmann, F.,Singleton, M.R.
Structural Basis of Eco1-Mediated Cohesin Acetylation.
Sci Rep, 7:44313-44313, 2017

PubMed Abstract: Sister-chromatid cohesion is established by Eco1-mediated acetylation on two conserved tandem lysines in the cohesin Smc3 subunit. However, the molecular basis of Eco1 substrate recognition and acetylation in cohesion is not fully understood. Here, we discover and rationalize the substrate specificity of Eco1 using mass spectrometry coupled with in-vitro acetylation assays and crystallography. Our structures of the X. laevis Eco2 (xEco2) bound to its primary and secondary Smc3 substrates demonstrate the plasticity of the substrate-binding site, which confers substrate specificity by concerted conformational changes of the central β hairpin and the C-terminal extension.

PubMed: 28290497
DOI: 10.1038/srep44313

実験手法

X-RAY DIFFRACTION (1.99 Å)