Crystallization and preliminary X-ray diffraction study of BchU, a methyltransferase from Chlorobium tepidum involved in bacteriochlorophyll c biosynthesis.
The S-adenosylmethionine-dependent methyltransferase BchU is an enzyme involved in the bacteriochlorophyll c biosynthetic pathway and catalyzes methylation at the C-20 position of the chlorin moiety. Recombinant Chlorobium tepidum BchU overproduced in Escherichia coli was purified and crystallized by the hanging-drop vapour-diffusion method using ammonium sulfate as a precipitant. The crystals belonged to the hexagonal space group P6(1)22 or P6(5)22, with unit-cell parameters a = b = 81.5, c = 250.7 A. A native data set was collected to 2.27 A resolution using synchrotron radiation at SPring-8.
Harada
Jiro
J
Department of Bioscience and Biotechnology, Faculty of Science and Engineering, Ritsumeikan University, Kusatsu, Shiga 525-8577, Japan.
Wada
Kei
K
Yamaguchi
Hitomi
H
Oh-oka
Hirozo
H
Tamiaki
Hitoshi
H
Fukuyama
Keiichi
K
D001426:Bacterial Proteins / Q000096:biosynthesis* / Q000737:chemistry; D001429:Bacteriochlorophylls / Q000096:biosynthesis* / Q000737:chemistry; D002384:Catalysis; D019414:Chlorobi / Q000378:metabolism*; D018360:Crystallography, X-Ray; D004058:Diffusion; D004926:Escherichia coli / Q000378:metabolism; D008745:Methylation; D008780:Methyltransferases / Q000737:chemistry*; D015233:Models, Statistical; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry; D017356:Synchrotrons; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D001429:Bacteriochlorophylls; D011994:Recombinant Proteins; C002084:bacteriochlorophyll c; D008780:Methyltransferases