2IXO

CRYSTAL STRUCTURE OF THE PP2A PHOSPHATASE ACTIVATOR Ypa1 PTPA1

2IXO の概要

• エントリーDOI: 10.2210/pdb2ixo/pdb
• 関連するPDBエントリー: 2IXP
• 分子名称: SERINE/THREONINE-PROTEIN PHOSPHATASE 2A ACTIVATOR 1 (2 entities in total)
• 機能のキーワード: isomerase, pp2a phosphatase activator prolyl isomerase ptpa, nuclear protein
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 74973.70

構造登録者

Leulliot, N.,Vicentini, G.,Jordens, J.,Quevillon-Cheruel, S.,Schiltz, M.,Barford, D.,Van Tilbeurgh, H.,Goris, J. (登録日: 2006-07-09, 公開日: 2006-07-31, 最終更新日: 2024-05-08)

主引用文献

Leulliot, N.,Vicentini, G.,Jordens, J.,Quevillon-Cheruel, S.,Schiltz, M.,Barford, D.,Van Tilbeurgh, H.,Goris, J.
Crystal Structure of the Pp2A Phosphatase Activator: Implications for its Pp2A-Specific Ppiase Activity.
Mol.Cell, 23:413-, 2006

PubMed Abstract: PTPA, an essential and specific activator of protein phosphatase 2A (PP2A), functions as a peptidyl prolyl isomerase (PPIase). We present here the crystal structures of human PTPA and of the two yeast orthologs (Ypa1 and Ypa2), revealing an all alpha-helical protein fold that is radically different from other PPIases. The protein is organized into two domains separated by a groove lined by highly conserved residues. To understand the molecular mechanism of PTPA activity, Ypa1 was cocrystallized with a proline-containing PPIase peptide substrate. In the complex, the peptide binds at the interface of a peptide-induced dimer interface. Conserved residues of the interdomain groove contribute to the peptide binding site and dimer interface. Structure-guided mutational studies showed that in vivo PTPA activity is influenced by mutations on the surface of the peptide binding pocket, the same mutations that also influenced the in vitro activation of PP2Ai and PPIase activity.

PubMed: 16885030
DOI: 10.1016/J.MOLCEL.2006.07.008

実験手法

X-RAY DIFFRACTION (2.6 Å)