5THY

Crystal structure of SeMet-Substituted CurJ carbon methyltransferase

5THY の概要

• エントリーDOI: 10.2210/pdb5thy/pdb
• 関連するPDBエントリー: 5THZ
• 分子名称: CurJ, S-ADENOSYL-L-HOMOCYSTEINE, OXIDIZED GLUTATHIONE DISULFIDE, ... (4 entities in total)
• 機能のキーワード: methyltransferase, transferase, lyase
• 由来する生物種: Moorea producens 3L
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 92300.15

構造登録者

Skiba, M.A.,Smith, J.L. (登録日: 2016-09-30, 公開日: 2016-10-19, 最終更新日: 2024-11-06)

主引用文献

Skiba, M.A.,Sikkema, A.P.,Fiers, W.D.,Gerwick, W.H.,Sherman, D.H.,Aldrich, C.C.,Smith, J.L.
Domain Organization and Active Site Architecture of a Polyketide Synthase C-methyltransferase.
ACS Chem. Biol., 11:3319-3327, 2016

PubMed Abstract: Polyketide metabolites produced by modular type I polyketide synthases (PKS) acquire their chemical diversity through the variety of catalytic domains within modules of the pathway. Methyltransferases are among the least characterized of the catalytic domains common to PKS systems. We determined the domain boundaries and characterized the activity of a PKS C-methyltransferase (C-MT) from the curacin A biosynthetic pathway. The C-MT catalyzes S-adenosylmethionine-dependent methyl transfer to the α-position of β-ketoacyl substrates linked to acyl carrier protein (ACP) or a small-molecule analog but does not act on β-hydroxyacyl substrates or malonyl-ACP. Key catalytic residues conserved in both bacterial and fungal PKS C-MTs were identified in a 2 Å crystal structure and validated biochemically. Analysis of the structure and the sequences bordering the C-MT provides insight into the positioning of this domain within complete PKS modules.

PubMed: 27723289
DOI: 10.1021/acschembio.6b00759

実験手法

X-RAY DIFFRACTION (2.087 Å)