3T7S
Crystal structure of complex of SAM and BVU_3255, a methyltransferase from Bacteroides vulgatus ATCC 8482
Summary for 3T7S
| Entry DOI | 10.2210/pdb3t7s/pdb |
| Related | 3T7R 3T7T |
| Descriptor | Putative methyltransferase, S-ADENOSYLMETHIONINE (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 | 4 |
| Total formula weight | 124252.61 |
| 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 Cited by 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: 21872662DOI: 10.1016/j.jsb.2011.08.007 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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