Crystallization and preliminary X-ray diffraction study of BchU, a methyltransferase from Chlorobium tepidum involved in bacteriochlorophyll c biosynthesis

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Jul 1;61(Pt 7):712-4. doi: 10.1107/S1744309105019093. Epub 2005 Jun 30.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / biosynthesis*
  • Bacterial Proteins / chemistry
  • Bacteriochlorophylls / biosynthesis*
  • Bacteriochlorophylls / chemistry
  • Catalysis
  • Chlorobi / metabolism*
  • Crystallography, X-Ray
  • Diffusion
  • Escherichia coli / metabolism
  • Methylation
  • Methyltransferases / chemistry*
  • Models, Statistical
  • Protein Conformation
  • Recombinant Proteins / chemistry
  • Synchrotrons
  • X-Ray Diffraction

Substances

  • Bacterial Proteins
  • Bacteriochlorophylls
  • Recombinant Proteins
  • bacteriochlorophyll c
  • Methyltransferases