6JLS

Crystal Structure of FMN-dependent Cysteine Decarboxylases TvaF from Thioviridamide Biosynthesis

6JLS の概要

• エントリーDOI: 10.2210/pdb6jls/pdb
• 分子名称: Putative flavoprotein decarboxylase, FLAVIN MONONUCLEOTIDE (3 entities in total)
• 機能のキーワード: fmn-dependent, biosynthetic protein
• 由来する生物種: Streptomyces olivoviridis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20860.54

構造登録者

Li, J.,Lu, J.,Wang, H.,Zhu, J. (登録日: 2019-03-06, 公開日: 2019-06-26, 最終更新日: 2023-11-22)

主引用文献

Lu, J.,Li, J.,Wu, Y.,Fang, X.,Zhu, J.,Wang, H.
Characterization of the FMN-Dependent Cysteine Decarboxylase from Thioviridamide Biosynthesis.
Org.Lett., 21:4676-4679, 2019

PubMed Abstract: The biosynthesis of thioviridamide-like compounds has not been elucidated. Herein, we report that TvaF from the thioviridamide biosynthetic gene cluster is an FMN-dependent cysteine decarboxylase that transforms the C-terminal cysteine of precursor peptides into a thioenol motif and exhibits high substrate flexibility. We resolved the crystal structure of TvaF bound with FMN at 2.24 Å resolution. Key residues for FMN binding and catalytic activity of TvaF have been identified and evaluated by mutagenesis studies.

PubMed: 31184189
DOI: 10.1021/acs.orglett.9b01531

実験手法

X-RAY DIFFRACTION (2.24 Å)