Crystallization and preliminary crystallographic studies of the catalytic subunits of human pyruvate dehydrogenase phosphatase isoforms 1 and 2

Junko Kato, Masato Kato

Research output: Contribution to journalArticle

2 Scopus citations

Abstract

Pyruvate dehydrogenase phosphatase (PDP) is a mitochondrial serine phos-phatase that activates phosphorylated pyruvate dehydrogenase complex by dephosphorylation. In humans, two PDP isoforms (1 and 2) have been identified. PDP1 is composed of a catalytic subunit (PDP1c) and a regulatory subunit (PDP1r), whereas PDP2 consists of only a catalytic subunit (PDP2c). Both PDP1c and PDP2c have been crystallized individually and complete X-ray diffraction data sets have been collected to 2.45 and 2.0 Å resolution, respectively. The PDP1c crystals belonged to space group P41212 or P43212, with unit-cell parameters a = b = 65.1, c = 216.1 Å. The asymmetric unit is expected to contain one molecule, with a Matthews coefficient VM of 2.56 Å3 Da-1. The PDP2c crystals belonged to space group P21212 1, with unit-cell parameters a = 53.6, b = 69.1, c = 109.7 Å. The asymmetric unit is expected to contain one molecule, with a Matthews coefficient VM of 1.91 Å3 Da-1.

Original languageEnglish (US)
Pages (from-to)342-345
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume66
Issue number3
DOIs
StatePublished - Mar 15 2010

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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