2npp
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(New page: 200px<br /> <applet load="2npp" size="450" color="white" frame="true" align="right" spinBox="true" caption="2npp, resolution 3.30Å" /> '''Structure of the Pr...)
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Revision as of 20:55, 12 November 2007
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Structure of the Protein Phosphatase 2A Holoenzyme
Overview
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.
About this Structure
2NPP is a Protein complex structure of sequences from Homo sapiens with MN as ligand. Active as Phosphoprotein phosphatase, with EC number 3.1.3.16 Full crystallographic information is available from OCA.
Reference
Structure of the protein phosphatase 2A holoenzyme., Xu Y, Xing Y, Chen Y, Chao Y, Lin Z, Fan E, Yu JW, Strack S, Jeffrey PD, Shi Y, Cell. 2006 Dec 15;127(6):1239-51. PMID:17174897
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