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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Mar 1;69(Pt 3):328-31. doi: 10.1107/S1744309113003837. Epub 2013 Feb 27.

Preliminary X-ray diffraction analysis of octaprenyl pyrophosphate synthase from Escherichia coli.

Author information

1
Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, Tianjin University of Science and Technology, Tianjin 300457, People's Republic of China.

Abstract

Octaprenyl pyrophosphate synthase (OPPs), which belongs to the E-type prenyltransferase family, catalyses the successive condensation of farnesyl pyrophosphate with five isopentenyl pyrophosphate molecules to form trans-C40-octaprenyl pyrophosphate (OPP). OPP is essential for the biosynthesis of bacterial ubiquinone or menaquinone side chains, which play an important role in the electron-transport system. Here, Escherichia coli OPPs was expressed, purified and crystallized. The crystals, which belonged to the orthorhombic space group P2₁2₁2, with unit-cell parameters a=117.0, b=128.4, c=46.4 Å, were obtained by the sitting-drop vapour-diffusion method and diffracted to 2.2 Å resolution. Initial phase determination by molecular replacement (MR) clearly indicated that the crystal contained one homodimer per asymmetric unit. Further model building and structural refinement are in progress.

KEYWORDS:

Escherichia coli; octaprenyl pyrophosphate; octaprenyl pyrophosphate synthase; prenyltransferase

PMID:
23519815
PMCID:
PMC3606585
DOI:
10.1107/S1744309113003837
[Indexed for MEDLINE]
Free PMC Article
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