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1. Structural and biochemical characterization of human PR70 in isolation and in complex with the scaffolding subunit of protein phosphatase 2A.

Author

Rebecca Dovega, Susan Tsutakawa, Esben M Quistgaard, Madhanagopal Anandapadamanaban, Christian Löw, and Pär Nordlund

Subjects
Medicine, Science
Abstract

Protein Phosphatase 2A (PP2A) is a major Ser/Thr phosphatase involved in the regulation of various cellular processes. PP2A assembles into diverse trimeric holoenzymes, which consist of a scaffolding (A) subunit, a catalytic (C) subunit and various regulatory (B) subunits. Here we report a 2.0 Å crystal structure of the free B''/PR70 subunit and a SAXS model of an A/PR70 complex. The crystal structure of B''/PR70 reveals a two domain elongated structure with two Ca2+ binding EF-hands. Furthermore, we have characterized the interaction of both binding partner and their calcium dependency using biophysical techniques. Ca2+ biophysical studies with Circular Dichroism showed that the two EF-hands display different affinities to Ca2+. In the absence of the catalytic C-subunit, the scaffolding A-subunit remains highly mobile and flexible even in the presence of the B''/PR70 subunit as judged by SAXS. Isothermal Titration Calorimetry studies and SAXS data support that PR70 and the A-subunit have high affinity to each other. This study provides additional knowledge about the structural basis for the function of B'' containing holoenzymes.

Published
2014
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2. Structural and biochemical characterization of Human PR70 in isolation and in complex with the scaffolding subunit of protein phosphatase 2A

Author

Pär Nordlund, Christian Löw, Madhanagopal Anandapadamanaban, Susan E. Tsutakawa, Rebecca Dovega, Esben M. Quistgaard, Soares, Claudio M., and School of Biological Sciences

Subjects
Proteomics, Models, Molecular, Protein Structure, Circular dichroism, Protein subunit, Phosphatase, lcsh:Medicine, Crystallography, X-Ray, Bioinformatics, Biochemistry, Protein Chemistry, Protein Structure, Secondary, Protein structure, X-Ray Diffraction, Holoenzymes, Scattering, Small Angle, Macromolecular Structure Analysis, Humans, Protein Phosphatase 2, Binding site, lcsh:Science, Protein Interactions, Molecular Biology, Macromolecular Complex Analysis, Spectrometric Identification of Proteins, Binding Sites, Multidisciplinary, Chemistry, Circular Dichroism, lcsh:R, Biology and Life Sciences, Proteins, Protein Complexes, Isothermal titration calorimetry, Protein phosphatase 2, Kemi, Recombinant Proteins, Science::Biological sciences [DRNTU], Protein-Protein Interactions, Chemical Sciences, Biophysics, lcsh:Q, Calcium, Protein Structure Determination, Protein Multimerization, Research Article
Abstract

Protein Phosphatase 2A (PP2A) is a major Ser/Thr phosphatase involved in the regulation of various cellular processes. PP2A assembles into diverse trimeric holoenzymes, which consist of a scaffolding (A) subunit, a catalytic (C) subunit and various regulatory (B) subunits. Here we report a 2.0 Å crystal structure of the free B’’/PR70 subunit and a SAXS model of an A/PR70 complex. The crystal structure of B’’/PR70 reveals a two domain elongated structure with two Ca2+ binding EF-hands. Furthermore, we have characterized the interaction of both binding partner and their calcium dependency using biophysical techniques. Ca2+ biophysical studies with Circular Dichroism showed that the two EF-hands display different affinities to Ca2+. In the absence of the catalytic C-subunit, the scaffolding A-subunit remains highly mobile and flexible even in the presence of the B’’/PR70 subunit as judged by SAXS. Isothermal Titration Calorimetry studies and SAXS data support that PR70 and the A-subunit have high affinity to each other. This study provides additional knowledge about the structural basis for the function of B’’ containing holoenzymes. Published version

Published
2014

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