2IE4

Structure of the Protein Phosphatase 2A Core Enzyme Bound to okadaic acid

Summary for 2IE4

• Entry DOI: 10.2210/pdb2ie4/pdb
• Related: 2IE3
• Descriptor: Protein Phosphatase 2, regulatory subunit A (PR 65), alpha isoform, Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform, MANGANESE (II) ION, ... (5 entities in total)
• Functional Keywords: protein-protein complex, heat repeat, signaling protein, hydrolase
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: P67775
• Total number of polymer chains: 2
• Total formula weight: 101929.38

Authors

Xing, Y.,Xu, Y.,Chen, Y.,Jeffrey, P.D.,Chao, Y.,Shi, Y. (deposition date: 2006-09-17, release date: 2006-11-07, Last modification date: 2024-02-21)

Primary citation

Xing, Y.,Xu, Y.,Chen, Y.,Jeffrey, P.D.,Chao, Y.,Lin, Z.,Li, Z.,Strack, S.,Stock, J.B.,Shi, Y.
Structure of Protein Phosphatase 2A Core Enzyme Bound to Tumor-Inducing Toxins
Cell(Cambridge,Mass.), 127:341-353, 2006

PubMed Abstract: The serine/threonine phosphatase protein phosphatase 2A (PP2A) plays an essential role in many aspects of cellular functions and has been shown to be an important tumor suppressor. The core enzyme of PP2A comprises a 65 kDa scaffolding subunit and a 36 kDa catalytic subunit. Here we report the crystal structures of the PP2A core enzyme bound to two of its inhibitors, the tumor-inducing agents okadaic acid and microcystin-LR, at 2.6 and 2.8 A resolution, respectively. The catalytic subunit recognizes one end of the elongated scaffolding subunit by interacting with the conserved ridges of HEAT repeats 11-15. Formation of the core enzyme forces the scaffolding subunit to undergo pronounced structural rearrangement. The scaffolding subunit exhibits considerable conformational flexibility, which is proposed to play an essential role in PP2A function. These structures, together with biochemical analyses, reveal significant insights into PP2A function and serve as a framework for deciphering the diverse roles of PP2A in cellular physiology.

PubMed: 17055435
DOI: 10.1016/j.cell.2006.09.025

Experimental method

X-RAY DIFFRACTION (2.6 Å)