6G86

Structure of Cdc14 bound to SIC1 PxL motif

6G86 の概要

• エントリーDOI: 10.2210/pdb6g86/pdb
• 分子名称: Tyrosine-protein phosphatase CDC14, Protein SIC1, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (7 entities in total)
• 機能のキーワード: cdc14, phosphatase, pxl, sic1, cell cycle
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 91192.56

構造登録者

Mouilleron, S.,Kataria, M.,Uhlmann, F. (登録日: 2018-04-07, 公開日: 2018-10-17, 最終更新日: 2025-10-01)

主引用文献

Kataria, M.,Mouilleron, S.,Seo, M.H.,Corbi-Verge, C.,Kim, P.M.,Uhlmann, F.
A PxL motif promotes timely cell cycle substrate dephosphorylation by the Cdc14 phosphatase.
Nat. Struct. Mol. Biol., 25:1093-1102, 2018

PubMed Abstract: The cell division cycle consists of a series of temporally ordered events. Cell cycle kinases and phosphatases provide key regulatory input, but how the correct substrate phosphorylation and dephosphorylation timing is achieved is incompletely understood. Here we identify a PxL substrate recognition motif that instructs dephosphorylation by the budding yeast Cdc14 phosphatase during mitotic exit. The PxL motif was prevalent in Cdc14-binding peptides enriched in a phage display screen of native disordered protein regions. PxL motif removal from the Cdc14 substrate Cbk1 delays its dephosphorylation, whereas addition of the motif advances dephosphorylation of otherwise late Cdc14 substrates. Crystal structures of Cdc14 bound to three PxL motif substrate peptides provide a molecular explanation for PxL motif recognition on the phosphatase surface. Our results illustrate the sophistication of phosphatase-substrate interactions and identify them as an important determinant of ordered cell cycle progression.

PubMed: 30455435
DOI: 10.1038/s41594-018-0152-3

実験手法

X-RAY DIFFRACTION (1.74 Å)