3T7R

Crystal structure of apo BVU_3255, a methyltransferase from Bacteroides vulgatus ATCC 8482

Summary for 3T7R

• Entry DOI: 10.2210/pdb3t7r/pdb
• Related: 3E7P 3T7S 3T7T
• Descriptor: Putative methyltransferase, 3-[(2Z)-3-methylpent-2-en-1-yl]benzene-1,2-diol (3 entities in total)
• Functional Keywords: small molecule methyltransferase, bvu_3255, rossmann fold, methyltrasnferase, sam, methylation, transferase
• Biological source: Bacteroides vulgatus
• Total number of polymer chains: 2
• Total formula weight: 61713.94

Authors

Kumar, V.,Sivaraman, J. (deposition date: 2011-07-31, release date: 2011-10-12, Last modification date: 2023-11-01)

Primary citation

Kumar, V.,Sivaraman, J.
Structural characterization of BVU_3255, a methyltransferase from human intestine antibiotic resistant pathogen Bacteroides vulgatus
J.Struct.Biol., 2011

PubMed 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.

PubMed: 21872662
DOI: 10.1016/j.jsb.2011.08.007

Experimental method

X-RAY DIFFRACTION (2.9 Å)