7WVZ

CalA3_modular PKS_KS-AT-DH-KR

7WVZ の概要

• エントリーDOI: 10.2210/pdb7wvz/pdb
• EMDBエントリー: 32863
• 分子名称: Beta-ketoacyl-acyl-carrier-protein synthase I (1 entity in total)
• 機能のキーワード: megaenzyme, hydrolase, transferase
• 由来する生物種: Streptomyces chartreusis NRRL 3882
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 361053.91

構造登録者

Wang, J.,Wang, Z. (登録日: 2022-02-12, 公開日: 2023-02-22, 最終更新日: 2023-10-11)

主引用文献

Wang, J.,Wang, X.,Li, X.,Kong, L.,Du, Z.,Li, D.,Gou, L.,Wu, H.,Cao, W.,Wang, X.,Lin, S.,Shi, T.,Deng, Z.,Wang, Z.,Liang, J.
C-N bond formation by a polyketide synthase.
Nat Commun, 14:1319-1319, 2023

PubMed Abstract: Assembly-line polyketide synthases (PKSs) are molecular factories that produce diverse metabolites with wide-ranging biological activities. PKSs usually work by constructing and modifying the polyketide backbone successively. Here, we present the cryo-EM structure of CalA3, a chain release PKS module without an ACP domain, and its structures with amidation or hydrolysis products. The domain organization reveals a unique "∞"-shaped dimeric architecture with five connected domains. The catalytic region tightly contacts the structural region, resulting in two stabilized chambers with nearly perfect symmetry while the N-terminal docking domain is flexible. The structures of the ketosynthase (KS) domain illustrate how the conserved key residues that canonically catalyze C-C bond formation can be tweaked to mediate C-N bond formation, revealing the engineering adaptability of assembly-line polyketide synthases for the production of novel pharmaceutical agents.

PubMed: 36899013
DOI: 10.1038/s41467-023-36989-w

実験手法

ELECTRON MICROSCOPY (3.38 Å)