Crystal structure of the catalytic subunit of bovine pyruvate dehydrogenase phosphatase.

ABSTRACT: Mammalian pyruvate dehydrogenase (PDH) activity is tightly regulated by phosphorylation and dephosphorylation, which is catalyzed by PDH kinase isomers and PDH phosphatase isomers, respectively. PDH phosphatase isomer 1 (PDP1) is a heterodimer consisting of a catalytic subunit (PDP1c) and a regulatory subunit (PDP1r). Here, the crystal structure of bovine PDP1c determined at 2.1 Å resolution is reported. The crystals belonged to space group P3₂21, with unit-cell parameters a = b = 75.3, c = 173.2 Å. The structure was solved by molecular-replacement methods and refined to a final R factor of 21.9% (R_free = 24.7%). The final model consists of 402 of a possible 467 amino-acid residues of the PDP1c monomer, two Mn²⁺ ions in the active site, an additional Mn

SUBMITTER: Guo Y 

PROVIDER: S-EPMC7336360 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature