Crystallization and preliminary X-ray analysis of isopentenyl diphosphate isomerase from Methanocaldococcus jannaschii

Takeshi Hoshino, Eriko Nango, Seiki Baba, Tadashi Eguchi, Takashi Kumasaka

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

Type 2 isopentenyl diphosphate isomerase (IDI-2) is a flavoprotein. Recently, flavin has been proposed to play a role as a general acid-base catalyst with no redox role during the enzyme reaction. To clarify the detailed enzyme reaction mechanism of IDI-2 and the unusual role of flavin, structural analysis of IDI-2 from Methanocaldococcus jannaschii (MjIDI) was performed. Recombinant MjIDI was crystallized at 293 K using calcium acetate as a precipitant. The diffraction of the crystal extended to 2.08 Å resolution at 100 K. The crystal belonged to the tetragonal space group I422, with unit-cell parameters a = 126.46, c = 120.03 Å. The presence of one monomer per asymmetric unit gives a crystal volume per protein weight (V M) of 3.0 Å3 Da-1 and a solvent constant of 59.0% by volume.

Original languageEnglish
Pages (from-to)101-103
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume67
Issue number1
DOIs
Publication statusPublished - 2011 Jan 1
Externally publishedYes

Keywords

  • flavoproteins
  • isopentenyl diphosphate isomerase
  • no net redox reaction

ASJC Scopus subject areas

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

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