8ZVG

Crystal structure of AetD in complex with L-tyrosine

8ZVG の概要

• エントリーDOI: 10.2210/pdb8zvg/pdb
• 分子名称: AetD, FE (II) ION, TYROSINE, ... (5 entities in total)
• 機能のキーワード: nitrile synthase, iron-dependent, l-tyrosine, metal binding protein
• 由来する生物種: Aetokthonos hydrillicola Thurmond2011
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 58182.73

構造登録者

Li, H.,Dai, L.,Zheng, H.B.,Chen, C.-C.,Guo, R.-T. (登録日: 2024-06-11, 公開日: 2024-10-02, 最終更新日: 2024-12-18)

主引用文献

Chen, C.C.,Li, H.,Huang, J.W.,Guo, R.T.
Structural and molecular insights of two unique enzymes involved in the biosynthesis of a natural halogenated nitrile.
Febs J., 291:5123-5132, 2024

PubMed Abstract: Organohalogen compounds exhibit wide-ranging bioactivities and potential applications. Understanding natural biosynthetic pathways and improving the production of halogenated compounds has garnered significant attention. Recently, the biosynthetic pathway of a cyanobacterial neurotoxin, aetokthonotoxin, was reported. It contains two unique enzymes: a single-component flavin-dependent halogenase AetF and a new type of nitril synthase AetD. The crystal structures of these enzymes in complex with their cofactors and substrates that were recently reported will be presented here. The AetF structures reveal a tri-domain architecture, the transfer direction of the hydride ion, a possible path to deliver the hypohalous acid, and the unusual bispecific substrate-recognition mode. The AetD structures demonstrate that the nitrile formation should occur through the action of a diiron cluster, implying that the enzyme should be capable of catalyzing the nitrile formation of alternative amino acids. This information is of central importance for understanding the mechanism of action as well as the applications of these two the-first-of-its-kind enzymes.

PubMed: 39308083
DOI: 10.1111/febs.17279

実験手法

X-RAY DIFFRACTION (1.89 Å)