Open AccessCrystallization and preliminary X‐ray analysis of isopentenyl diphosphate isomerase from Methanocaldococcus jannaschii
Author(s) -
Hoshino Takeshi,
Nango Eriko,
Baba Seiki,
Eguchi Tadashi,
Kumasaka Takashi
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110046944
Subject(s) - isomerase , crystallization , flavin group , flavoprotein , tetragonal crystal system , chemistry , flavin adenine dinucleotide , stereochemistry , dimer , enzyme , crystallography , crystal structure , biochemistry , organic chemistry , cofactor
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 I 422, 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 Å 3 Da −1 and a solvent constant of 59.0% by volume.