Journal:Acta Cryst D:S2059798322008373

spinqualitylabelsall models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D 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 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. The two subunits of NfsB dimer are shown in green and cyan, respectively. The molecules FMN, BBR and DMSO are shown as state blue, magenta and yellow ball-and-sticks, respectively. 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. Water molecules are shown as red spheres. All berberine interactions. A proposed mechanism of BBR-to-dhBBR conversion by bacterial NRs Remember to drag the structures with the mouse to rotate them. References

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