2NPP

Structure of the Protein Phosphatase 2A Holoenzyme

Summary for 2NPP

• Entry DOI: 10.2210/pdb2npp/pdb
• Related: 2IE3 2IE4
• Related PRD ID: PRD_000212
• Descriptor: Protein Phosphatase 2, regulatory subunit A (PR 65), alpha isoform, Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform, Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform, ... (5 entities in total)
• Functional Keywords: heat repeat, signaling protein, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: P67775; Nucleus: Q13362
• Total number of polymer chains: 8
• Total formula weight: 309667.67

Authors

Xu, Y.,Chen, Y.,Xing, Y.,Chao, Y.,Shi, Y. (deposition date: 2006-10-28, release date: 2006-12-12, Last modification date: 2023-11-15)

Primary citation

Xu, Y.,Xing, Y.,Chen, Y.,Chao, Y.,Lin, Z.,Fan, E.,Yu, J.W.,Strack, S.,Jeffrey, P.D.,Shi, Y.
Structure of the protein phosphatase 2A holoenzyme
Cell(Cambridge,Mass.), 127:1239-1251, 2006

PubMed Abstract: Protein Phosphatase 2A (PP2A) plays an essential role in many aspects of cellular physiology. The PP2A holoenzyme consists of a heterodimeric core enzyme, which comprises a scaffolding subunit and a catalytic subunit, and a variable regulatory subunit. Here we report the crystal structure of the heterotrimeric PP2A holoenzyme involving the regulatory subunit B'/B56/PR61. Surprisingly, the B'/PR61 subunit has a HEAT-like (huntingtin-elongation-A subunit-TOR-like) repeat structure, similar to that of the scaffolding subunit. The regulatory B'/B56/PR61 subunit simultaneously interacts with the catalytic subunit as well as the conserved ridge of the scaffolding subunit. The carboxyterminus of the catalytic subunit recognizes a surface groove at the interface between the B'/B56/PR61 subunit and the scaffolding subunit. Compared to the scaffolding subunit in the PP2A core enzyme, formation of the holoenzyme forces the scaffolding subunit to undergo pronounced conformational rearrangements. This structure reveals significant ramifications for understanding the function and regulation of PP2A.

PubMed: 17174897
DOI: 10.1016/j.cell.2006.11.033

Experimental method

X-RAY DIFFRACTION (3.3 Å)