7A9I

Crystal structure of Coronafacic Acid Ligase from Pectobacterium brasiliense

7A9I の概要

• エントリーDOI: 10.2210/pdb7a9i/pdb
• 分子名称: Cfl, 6-ethyl-1-oxidanylidene-indene-4-carboxylic acid, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: ligase
• 由来する生物種: Pectobacterium brasiliense
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 60893.57

構造登録者

Levy, C.W. (登録日: 2020-09-02, 公開日: 2021-05-05, 最終更新日: 2024-05-01)

主引用文献

Winn, M.,Rowlinson, M.,Wang, F.,Bering, L.,Francis, D.,Levy, C.,Micklefield, J.
Discovery, characterization and engineering of ligases for amide synthesis.
Nature, 593:391-398, 2021

PubMed Abstract: Coronatine and related bacterial phytotoxins are mimics of the hormone jasmonyl-L-isoleucine (JA-Ile), which mediates physiologically important plant signalling pathways. Coronatine-like phytotoxins disrupt these essential pathways and have potential in the development of safer, more selective herbicides. Although the biosynthesis of coronatine has been investigated previously, the nature of the enzyme that catalyses the crucial coupling of coronafacic acid to amino acids remains unknown. Here we characterize a family of enzymes, coronafacic acid ligases (CfaLs), and resolve their structures. We found that CfaL can also produce JA-Ile, despite low similarity with the Jar1 enzyme that is responsible for ligation of JA and L-Ile in plants. This suggests that Jar1 and CfaL evolved independently to catalyse similar reactions-Jar1 producing a compound essential for plant development, and the bacterial ligases producing analogues toxic to plants. We further demonstrate how CfaL enzymes can be used to synthesize a diverse array of amides, obviating the need for protecting groups. Highly selective kinetic resolutions of racemic donor or acceptor substrates were achieved, affording homochiral products. We also used structure-guided mutagenesis to engineer improved CfaL variants. Together, these results show that CfaLs can deliver a wide range of amides for agrochemical, pharmaceutical and other applications.

PubMed: 34012085
DOI: 10.1038/s41586-021-03447-w

実験手法

X-RAY DIFFRACTION (2.1 Å)