| Literature DB >> 21872662 |
Veerendra Kumar1, J Sivaraman.
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. Copyright ÂEntities:
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Year: 2011 PMID: 21872662 DOI: 10.1016/j.jsb.2011.08.007
Source DB: PubMed Journal: J Struct Biol ISSN: 1047-8477 Impact factor: 2.867