Crystallization and structural analysis of GADPH from Spinacia oleracea in a new form

Ana Cámara-Artigas, Masakazu Hirasawa, David B. Knaff, Meitian Wang, James Allen

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

Abstract

Two crystalline forms of GADPH (d-glyceraldehyde-3-phosphate dehydrogenase) from Spinacia oleracea were obtained using sitting-drop vapor diffusion. Despite the very low concentration of GADPH in the solutions, two crystalline forms were obtained, one of which was the previously reported C222 space group with unit-cell parameters a = 155.3, b = 181.7, c = 107.6 Å and the other of which belonged to a new space group I4122, with unit-cell parameters a = b = 120.9, c = 154.5 Å. Diffraction data were measured from both native and derivatives, yielding structures at a resolution limit of 3.0 Å. Differences at the NAD+/NADP+-binding site seen in these structures compared with the previously reported structure with bound coenzyme suggest that conformational changes associated with pyridine-nucleotide binding may play a role in the regulation of this enzyme.

Original languageEnglish (US)
Pages (from-to)1087-1092
Number of pages6
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume62
Issue number11
DOIs
StatePublished - Nov 2006

Keywords

  • GADPH
  • Glutamate synthase
  • NAD/NADP

ASJC Scopus subject areas

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

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