6JLS

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

Summary for 6JLS

• Entry DOI: 10.2210/pdb6jls/pdb
• Descriptor: Putative flavoprotein decarboxylase, FLAVIN MONONUCLEOTIDE (3 entities in total)
• Functional Keywords: fmn-dependent, biosynthetic protein
• Biological source: Streptomyces olivoviridis
• Total number of polymer chains: 1
• Total formula weight: 20860.54

Authors

Li, J.,Lu, J.,Wang, H.,Zhu, J. (deposition date: 2019-03-06, release date: 2019-06-26, Last modification date: 2023-11-22)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.24 Å)