Journal:Acta Cryst D:S2059798322008373
From Proteopedia
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<b>Molecular Tour</b><br> | <b>Molecular Tour</b><br> | ||
| - | Crystal structure of bacterial nitroreductase (NR) NfsB in complex with the traditional medicine berberine (BBR) showed <scene name='92/920253/Cv/2'>BBR binds into the active pocket at the NfsB dimer interface</scene>. BBR is mainly stabilized by <scene name='92/920253/Cv/3'>π-stacking interactions with both neighboring aromatic residues and the cofactor FMN</scene>. Several well-ordered <scene name='92/920253/Cv/4'>water molecules neighboring BBR in the active site</scene> probably donate protons in conjunction with electron transfer from FMN for BBR reduction. | + | Crystal structure of bacterial nitroreductase (NR) NfsB in complex with the traditional medicine berberine (BBR) showed <scene name='92/920253/Cv/2'>BBR binds into the active pocket at the NfsB dimer interface</scene>. 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 <scene name='92/920253/Cv/3'>π-stacking interactions with both neighboring aromatic residues and the cofactor FMN</scene>. Several well-ordered <scene name='92/920253/Cv/4'>water molecules neighboring BBR in the active site</scene> probably donate protons in conjunction with electron transfer from FMN for BBR reduction. Water molecules are shown as red spheres. |
[[Image:NRpathway.png|left|350px|thumb|A proposed mechanism of BBR-to-dhBBR conversion by bacterial NRs]] | [[Image:NRpathway.png|left|350px|thumb|A proposed mechanism of BBR-to-dhBBR conversion by bacterial NRs]] | ||
{{Clear}} | {{Clear}} | ||
Revision as of 07:31, 24 August 2022
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This page complements a publication in scientific journals and is one of the Proteopedia's Interactive 3D Complement pages. For aditional details please see I3DC.
