3X21

Crystal structure of Escherichia coli nitroreductase NfsB mutant T41L/N71S/F124W

Summary for 3X21

• Entry DOI: 10.2210/pdb3x21/pdb
• Related: 1DS7 3X22
• Descriptor: Oxygen-insensitive NAD(P)H nitroreductase, FLAVIN MONONUCLEOTIDE (3 entities in total)
• Functional Keywords: nitroreductase, regioselectivity, dinitrocompounds, oxidoreductase
• Biological source: Escherichia coli K-12
• Total number of polymer chains: 10
• Total formula weight: 265889.59

Authors

Bai, J.,Yang, J.,Zhou, Y.,Yang, Q. (deposition date: 2014-12-06, release date: 2015-05-20, Last modification date: 2023-11-08)

Primary citation

Bai, J.,Zhou, Y.,Chen, Q.,Yang, Q.,Yang, J.
Altering the regioselectivity of a nitroreductase in the synthesis of arylhydroxylamines by structure-based engineering.
Chembiochem, 16:1219-1225, 2015

PubMed Abstract: Nitroreductases have great potential for the highly efficient reduction of aryl nitro compounds to arylhydroxylamines. However, regioselective reduction of the desired nitro group in polynitroarenes is still a challenge. Here, we describe the structure-based engineering of Escherichia coli nitroreductase NfsB to alter its regioselectivity, in order to achieve reduction of a target nitro group. When 2,4-dinitrotoluene was used as the substrate, the wild-type enzyme regioselectively reduced the 4-NO2 group, but the T41L/N71S/F124W mutant primarily reduced the 2-NO2 group, without loss of activity. The crystal structure of T41L/N71S/F124W and docking experiments indicated that the regioselectivity change (from 4-NO2 to 2-NO2 ) might result from the increased hydrophobicity of residues 41 and 124 (proximal to FMN) and conformational changes in residues 70 and 124.

PubMed: 25917861
DOI: 10.1002/cbic.201500070

Experimental method

X-RAY DIFFRACTION (3.002 Å)