Crystallization and preliminary crystallographic studies of UbiG, an O-methyltransferase from Escherichia coli.

Abstract

UbiG, an O-methyltransferase from the ubiquinone-biosynthesis pathway in Escherichia coli, catalyzes two O-methyl transfer steps. The primary structures of the O-methyltransferase enzyme family used in ubiquinone synthesis are conserved in both prokaryotes and eukaryotes, but their tertiary structures and catalytic mechanisms are not yet known. Here, UbiG with an N-terminal hexahistidine tag was expressed and crystallized. Crystals grown by the hanging-drop vapour-diffusion method diffracted to 2.00 Å resolution and belonged to space group C121, with unit-cell parameters a = 119.8, b = 58.6, c = 40.2 Å, β = 105.3°. Both Matthews coefficient analysis and the self-rotation function suggested the presence of one molecule per asymmetric unit in the crystal, with a solvent content of 50.52% (V(M) = 2.48 Å(3) Da(-1)).

DOI: 10.1107/S1744309111014278

Cite this paper

@article{Xing2011CrystallizationAP, title={Crystallization and preliminary crystallographic studies of UbiG, an O-methyltransferase from Escherichia coli.}, author={Li Xing and Yuwei Zhu and Pengfei Fang and Jing Wang and Fuxing Zeng and Xuesong Li and Maikun Teng and Xu Li}, journal={Acta crystallographica. Section F, Structural biology and crystallization communications}, year={2011}, volume={67 Pt 6}, pages={727-9} }