期刊
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
卷 67, 期 -, 页码 727-729出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309111014278
关键词
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资金
- Fundamental Research Funds for the Central Universities
- Chinese National Natural Science Foundation [30900224, 10979039]
- Chinese Ministry of Science and Technology [2006AA02A318, 2009CB825500]
- Science and Technological Fund of Anhui Province for Outstanding Youth [10040606Y11]
- Anhui Provincial Natural Science Foundation [090413081]
- Education Department of Anhui Province [2009SQRZ007ZD]
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 angstrom resolution and belonged to space group C121, with unit-cell parameters a = 119.8, b = 58.6, c = 40.2 angstrom, beta = 105.3 degrees. 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 angstrom(3) Da(-1)).
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