3T7S

Crystal structure of complex of SAM and BVU_3255, a methyltransferase from Bacteroides vulgatus ATCC 8482

3T7S の概要

• エントリーDOI: 10.2210/pdb3t7s/pdb
• 関連するPDBエントリー: 3T7R 3T7T
• 分子名称: Putative methyltransferase, S-ADENOSYLMETHIONINE (3 entities in total)
• 機能のキーワード: small molecule methyltransferase, bvu_3255, rossmann fold, methyltrasnferase, sam, methylation, transferase
• 由来する生物種: Bacteroides vulgatus
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 124252.61

構造登録者

Kumar, V.,Sivaraman, J. (登録日: 2011-07-31, 公開日: 2011-10-12, 最終更新日: 2023-11-01)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.2 Å)