1OHC

Structure of the proline directed phosphatase cdc14

1OHC の概要

• エントリーDOI: 10.2210/pdb1ohc/pdb
• 関連するPDBエントリー: 1OHD 1OHE
• 分子名称: CDC14B2 PHOSPHATASE (2 entities in total)
• 機能のキーワード: dual specificity phosphatase, hydrolase
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40477.11

構造登録者

Gray, C.H.,Good, V.M.,Tonks, N.K.,Barford, D. (登録日: 2003-05-24, 公開日: 2003-07-24, 最終更新日: 2024-05-08)

主引用文献

Gray, C.H.,Good, V.M.,Tonks, N.K.,Barford, D.
The Structure of the Cell Cycle Protein Cdc14 Reveals a Proline-Directed Protein Phosphatase
Embo J., 22:3524-, 2003

PubMed Abstract: The Cdc14 family of dual-specificity protein phosphatases (DSPs) is conserved within eukaryotes and functions to down-regulate mitotic Cdk activities, promoting cytokinesis and mitotic exit. We have integrated structural and kinetic analyses to define the molecular mechanism of the dephosphorylation reaction catalysed by Cdc14. The structure of Cdc14 illustrates a novel arrangement of two domains, each with a DSP-like fold, arranged in tandem. The C-terminal domain contains the conserved PTP motif of the catalytic site, whereas the N-terminal domain, which shares no sequence similarity with other DSPs, contributes to substrate specificity, and lacks catalytic activity. The catalytic site is located at the base of a pronounced surface channel formed by the interface of the two domains, and regions of both domains interact with the phosphopeptide substrate. Specificity for a pSer-Pro motif is mediated by a hydrophobic pocket that is capable of accommodating the apolar Pro(P+1) residue of the peptide. Our structural and kinetic data support a role for Cdc14 in the preferential dephosphorylation of proteins modified by proline-directed kinases.

PubMed: 12853468
DOI: 10.1093/EMBOJ/CDG348

実験手法

X-RAY DIFFRACTION (2.5 Å)