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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, ? = 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)).

SUBMITTER: Xing L

PROVIDER: S-EPMC3107154 | biostudies-literature | 2011 Jun

REPOSITORIES: biostudies-literature

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

Xing Li L Zhu Yuwei Y Fang Pengfei P Wang Jing J Zeng Fuxing F Li Xuesong X Teng Maikun M Li Xu X

Acta crystallographica. Section F, Structural biology and crystallization communications 20110526 Pt 6

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 ...[more]

PMID: 21636923

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