5XW4

Crystal structure of budding yeast Cdc14p (wild type) in the apo state

5XW4 の概要

• エントリーDOI: 10.2210/pdb5xw4/pdb
• 分子名称: Tyrosine-protein phosphatase CDC14 (2 entities in total)
• 機能のキーワード: phosphatase, cell cycle
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
• 細胞内の位置: Nucleus, nucleolus: Q00684
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 95281.66

構造登録者

Kobayashi, J.,Matsuura, Y. (登録日: 2017-06-29, 公開日: 2017-08-09, 最終更新日: 2023-11-22)

主引用文献

Kobayashi, J.,Matsuura, Y.
Structure and dimerization of the catalytic domain of the protein phosphatase Cdc14p, a key regulator of mitotic exit in Saccharomyces cerevisiae
Protein Sci., 26:2105-2112, 2017

PubMed Abstract: In the budding yeast Saccharomyces cerevisiae, the protein phosphatase Cdc14p orchestrates various events essential for mitotic exit. We have determined the X-ray crystal structures at 1.85 Å resolution of the catalytic domain of Cdc14p in both the apo state, and as a complex with S160-phosphorylated Swi6p peptide. Each asymmetric unit contains two Cdc14p chains arranged in an intimately associated homodimer, consistent with its oligomeric state in solution. The dimerization interface is located on the backside of the substrate-binding cleft. Structure-based mutational analyses indicate that the dimerization of Cdc14p is required for normal growth of yeast cells.

PubMed: 28758351
DOI: 10.1002/pro.3244

実験手法

X-RAY DIFFRACTION (1.85 Å)