3N2S

Structure of NfrA1 nitroreductase from B. subtilis

Summary for 3N2S

• Entry DOI: 10.2210/pdb3n2s/pdb
• Descriptor: NADPH-dependent nitro/flavin reductase, FLAVIN MONONUCLEOTIDE, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: alpga-beta-alpha sandwich, oxidoreductase
• Biological source: Bacillus subtilis
• Total number of polymer chains: 4
• Total formula weight: 116628.78

Authors

Morera, S.,Gueguen-Chaignon, V.,Meyer, P.,Cortial, S.,Ouazzani, J. (deposition date: 2010-05-19, release date: 2010-09-15, Last modification date: 2024-11-06)

Primary citation

Cortial, S.,Chaignon, P.,Iorga, B.I.,Aymerich, S.,Truan, G.,Gueguen-Chaignon, V.,Meyer, P.,Morera, S.,Ouazzani, J.
NADH oxidase activity of Bacillus subtilis nitroreductase NfrA1: insight into its biological role.
Febs Lett., 584:3916-3922, 2010

PubMed Abstract: NfrA1 nitroreductase from the Gram-positive bacterium Bacillus subtilis is a member of the NAD(P)H/FMN oxidoreductase family. Here, we investigated the reactivity, the structure and kinetics of NfrA1, which could provide insight into the unclear biological role of this enzyme. We could show that NfrA1 possesses an NADH oxidase activity that leads to high concentrations of oxygen peroxide and an NAD(+) degrading activity leading to free nicotinamide. Finally, we showed that NfrA1 is able to rapidly scavenge H(2)O(2) produced during the oxidative process or added exogenously.

PubMed: 20727352
DOI: 10.1016/j.febslet.2010.08.019

Experimental method

X-RAY DIFFRACTION (1.95 Å)