Structural basis for the transformation of traditional medicine berberine by bacterial nitroreductase
Hai-Ying Wen, Li-Bin Pan, Shu-Rong Ma, Xin-Yu Yang, Jia-Chun Hu, Hai-Fan Zhao, Zeng-Qiang Gao, Yu-Hui Dong, Jian-Dong Jiang, Yan Wang and Heng Zhang [1]
Molecular Tour
Crystal structure of bacterial nitroreductase (NR) NfsB in complex with the traditional medicine berberine (BBR) showed BBR binds into the active pocket at the NfsB dimer interface. BBR is mainly stabilized by π-stacking interactions with both neighboring aromatic residues and the cofactor FMN. Several well-ordered water molecules neighboring BBR in the active site probably donate protons in conjunction with electron transfer from FMN for BBR reduction.
References
- ↑ Wen HY, Pan LB, Ma SR, Yang XY, Hu JC, Zhao HF, Gao ZQ, Dong YH, Wang Y, Zhang H. Structural basis for the transformation of the traditional medicine berberine by bacterial nitroreductase. Acta Crystallogr D Struct Biol. 2022 Oct 1;78(Pt 10):1273-1282. doi:, 10.1107/S2059798322008373. Epub 2022 Sep 27. PMID:36189746 doi:http://dx.doi.org/10.1107/S2059798322008373
