Correlation Engine 2.0
Clear Search sequence regions

Sizes of these terms reflect their relevance to your search.

Violacein is a pigment synthesized by gram-negative bacteria with various biological activities such as antimicrobial, antiviral, and anticancer activities. VioD is a key oxygenase converting protodeoxyviolaceinic acid to protoviolaceinic acid in violacein biosynthesis. To elucidate the catalytic mechanism of VioD, here, we resolved two crystal structures of VioD, a binary complex structure containing VioD and a FAD and a ternary complex structure composed of VioD, a FAD and a 2-ethyl-1-hexanol (EHN). Structural analysis revealed a deep funnel like binding pocket with wide entrance, this pocket is positively charged. The EHN is located at the deep bottom of the binding pocket near isoalloxazine ring. Further docking simulation help us to propose the mechanism of the hydroxylation of the substrate catalyzed by VioD. Bioinformatic analysis suggested and emphasized the importance of the conserved residues involved in substrate binding. Our results provide a structural basis for the catalytic mechanism of VioD. © 2023 Wiley Periodicals LLC.


Mengxue Xu, Dongqing Xu, Mengxiao Gao, Xuebo Zhuang, Weiwu Wang, Bo Sun, Tingting Ran. Structural basis for substrate binding and catalytic mechanism of the key enzyme VioD in the violacein synthesis pathway. Proteins. 2023 Jul;91(7):956-966

Expand section icon Mesh Tags

Expand section icon Substances

PMID: 36869636

View Full Text