5MGZ

Streptomyces Spheroides NovO (8-demethylnovbiocic acid methyltransferase) with SAH

5MGZ の概要

• エントリーDOI: 10.2210/pdb5mgz/pdb
• 分子名称: 8-demethylnovobiocic acid C(8)-methyltransferase, S-ADENOSYL-L-HOMOCYSTEINE, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: c methyltransferase, novobiocin biosynthesis, sam dependent, transferase
• 由来する生物種: Streptomyces niveus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 53435.12

構造登録者

Chung, C.-W.,Mosley, J.,Sadler, J.C. (登録日: 2016-11-22, 公開日: 2017-01-18, 最終更新日: 2024-05-08)

主引用文献

Sadler, J.C.,Chung, C.H.,Mosley, J.E.,Burley, G.A.,Humphreys, L.D.
Structural and Functional Basis of C-Methylation of Coumarin Scaffolds by NovO.
ACS Chem. Biol., 12:374-379, 2017

PubMed Abstract: C-methylation of aromatic small molecules by C-methyltransferases (C-MTs) is an important biological transformation that involves C-C bond formation using S-adenosyl-l-methionine (SAM) as the methyl donor. Here, two advances in the mechanistic understanding of C-methylation of the 8-position of coumarin substrates catalyzed by the C-MT NovO from Streptomyces spheroides are described. First, a crystal structure of NovO reveals the Arg116-Asn117 and His120-Arg121 motifs are essential for coumarin substrate binding. Second, the active-site His120 is responsible for deprotonation of the phenolic 7-hydroxyl group on the coumarin substrate, activating the rate-determining methyl transfer step from SAM. This work expands our mechanistic knowledge of C-MTs, which could be used in the downstream development of engineered biocatalysts for small molecule C-alkylations.

PubMed: 28068060
DOI: 10.1021/acschembio.6b01053

実験手法

X-RAY DIFFRACTION (1.9 Å)