Structural characterization of BVU_3255, a methyltransferase from human intestine antibiotic resistant pathogen Bacteroides vulgatus

J Struct Biol. 2011 Dec;176(3):409-13. doi: 10.1016/j.jsb.2011.08.007. Epub 2011 Aug 22.


Methylation is important for various cellular activities. To date, there is no report of any methyltransferase structure from the human intestine antibiotic resistant pathogen Bacteroides vulgatus. The protein BVU_3255 from B. vulgatus ATCC 8482 belongs to a SAM-dependent methyltransferase. Here, we report the crystal structure of apo BVU_3255, and its complexes with SAM and SAH, which revealed a typical class I Rossmann Fold Methyltransferase. Isothermal titration calorimetric studies showed that both SAM and SAH bind with equal affinity. The structural and sequence analysis suggested that BVU_3255 is a small molecule methyltransferase and involved in methylating the intermediates in ubiquinone biosynthesis pathway.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacteroides / enzymology*
  • Binding Sites
  • Catalytic Domain
  • Crystallography, X-Ray
  • Drug Resistance, Bacterial
  • Humans
  • Intestines / microbiology*
  • Methylation
  • Methyltransferases / chemistry*
  • Protein Folding
  • Protein Structure, Secondary
  • S-Adenosylhomocysteine / chemistry
  • S-Adenosylmethionine / chemistry
  • Ubiquinone / biosynthesis


  • Bacterial Proteins
  • Ubiquinone
  • S-Adenosylmethionine
  • S-Adenosylhomocysteine
  • Methyltransferases