Conformational Changes in Active and Inactive States of Human PP2Cα Characterized by Hydrogen/Deuterium Exchange-Mass Spectrometry.

ABSTRACT: PPM serine/threonine protein phosphatases function in signaling pathways and require millimolar concentrations of Mn²⁺ or Mg²⁺ ions for activity. Whereas the crystal structure of human PP2Cα displayed two tightly bound Mn²⁺ ions in the active site, recent investigations of PPM phosphatases have characterized the binding of a third, catalytically essential metal ion. The binding of the third Mg²⁺ to PP2Cα was reported to have millimolar affinity and to be entropically driven, suggesting it may be structurally and catalytically important. Here, we report the use of hydrogen/deuterium exchange-mass spectrometry and molecular dynamics to characterize conformational changes in PP2Cα between the active and inactive states. In the presence of millimolar

SUBMITTER: Mazur SJ 

PROVIDER: S-EPMC5593270 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature