title: Structural characterization of BVU_3255, a methyltransferase from human intestine antibiotic resistant pathogen Bacteroides vulgatus.
abstract: 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.
authors.affiliation: Department of Biological Sciences, National University of Singapore, Singapore, Republic of Singapore.
authors.forename: Veerendra
authors.initials: V
authors.lastname: Kumar
authors.forename: J
authors.initials: J
authors.lastname: Sivaraman
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D001439:Bacteroides / Q000201:enzymology*; D001665:Binding Sites; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D024881:Drug Resistance, Bacterial; D006801:Humans; D007422:Intestines / Q000382:microbiology*; D008745:Methylation; D008780:Methyltransferases / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D012435:S-Adenosylhomocysteine / Q000737:chemistry; D012436:S-Adenosylmethionine / Q000737:chemistry; D014451:Ubiquinone / Q000096:biosynthesis
chemical_list: D001426:Bacterial Proteins; D014451:Ubiquinone; D012436:S-Adenosylmethionine; D012435:S-Adenosylhomocysteine; D008780:Methyltransferases