6CCA

Crystal structure of DszA carbon methyltransferase

6CCA の概要

• エントリーDOI: 10.2210/pdb6cca/pdb
• 分子名称: DisA protein (2 entities in total)
• 機能のキーワード: methyltransferase, polyketide assembly line, disorazol, gem-dimethyl, transferase
• 由来する生物種: Sorangium cellulosum (Polyangium cellulosum)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 47334.79

構造登録者

Meinke, J.L.,Keatinge-Clay, A.T. (登録日: 2018-02-06, 公開日: 2018-12-05, 最終更新日: 2024-03-13)

主引用文献

Meinke, J.L.,Mehaffey, M.R.,Wagner, D.T.,Sun, N.,Zhang, Z.,Brodbelt, J.S.,Keatinge-Clay, A.T.
Structural and Functional Studies of a gem-Dimethylating Methyltransferase from a trans-Acyltransferase Assembly Line.
ACS Chem. Biol., 13:3306-3314, 2018

PubMed Abstract: The methyl substituents in products of trans-acyltransferase assembly lines are usually incorporated by S-adenosyl-methionine (SAM)-dependent methyltransferase (MT) domains. The gem-dimethyl moieties within the polyketide disorazol are installed through the iterative action of an MT in the third module of its assembly line. The 1.75-Å-resolution crystal structure of this MT helps elucidate how it catalyzes the addition of two methyl groups. Activity assays of point mutants on β-ketoacyl chains linked to an acyl carrier protein and N-acetylcysteamine provide additional insights into the roles of active site residues. The replacement of an alanine with a phenylalanine at an apparent gatekeeping position resulted in more monomethylation than dimethylation. MTs may form an interface with ketoreductases (KRs) and even mediate the docking of trans-acyltransferase assembly line polypeptides through this association.

PubMed: 30371052
DOI: 10.1021/acschembio.8b00733

実験手法

X-RAY DIFFRACTION (1.75 Å)