6jls

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

spinqualitylabelsall models 6jls, resolution 2.24Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6jls is a 1 chain structure with sequence from Streptomyces olivoviridis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.24Å Ligands: FMN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function T2HUM4_9ACTN Publication Abstract from PubMed 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 A resolution. Key residues for FMN binding and catalytic activity of TvaF have been identified and evaluated by mutagenesis studies. Characterization of the FMN-Dependent Cysteine Decarboxylase from Thioviridamide Biosynthesis.,Lu J, Li J, Wu Y, Fang X, Zhu J, Wang H Org Lett. 2019 Jun 3. doi: 10.1021/acs.orglett.9b01531. PMID:31184189 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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