4WSF

Falafel EVH1 domain bound to CENP-C FIM

4WSF の概要

• エントリーDOI: 10.2210/pdb4wsf/pdb
• 分子名称: Serine/threonine-protein phosphatase 4 regulatory subunit 3, Cenp-C, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: phosphatase evh1 domain, signaling protein
• 由来する生物種: Drosophila melanogaster (Fruit fly); 詳細
• 細胞内の位置: Nucleus : Q9VFS5
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 16107.74

構造登録者

Lefevre, S.R.,Singleton, M.R. (登録日: 2014-10-27, 公開日: 2014-12-10, 最終更新日: 2024-01-10)

主引用文献

Lipinszki, Z.,Lefevre, S.,Savoian, M.S.,Singleton, M.R.,Glover, D.M.,Przewloka, M.R.
Centromeric binding and activity of Protein Phosphatase 4.
Nat Commun, 6:5894-5894, 2015

PubMed Abstract: The cell division cycle requires tight coupling between protein phosphorylation and dephosphorylation. However, understanding the cell cycle roles of multimeric protein phosphatases has been limited by the lack of knowledge of how their diverse regulatory subunits target highly conserved catalytic subunits to their sites of action. Phosphoprotein phosphatase 4 (PP4) has been recently shown to participate in the regulation of cell cycle progression. We now find that the EVH1 domain of the regulatory subunit 3 of Drosophila PP4, Falafel (Flfl), directly interacts with the centromeric protein C (CENP-C). Unlike other EVH1 domains that interact with proline-rich ligands, the crystal structure of the Flfl amino-terminal EVH1 domain bound to a CENP-C peptide reveals a new target-recognition mode for the phosphatase subunit. We also show that binding of Flfl to CENP-C is required to bring PP4 activity to centromeres to maintain CENP-C and attached core kinetochore proteins at chromosomes during mitosis.

PubMed: 25562660
DOI: 10.1038/ncomms6894

実験手法

X-RAY DIFFRACTION (1.501 Å)