Open AccessCrystallization and preliminary crystallographic analysis of a flavoprotein NADH oxidase from Lactobacillus brevis
Author(s) -
Kuzu Mutlu,
Niefind Karsten,
Hummel Werner,
Schomburg Dietmar
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430910501153x
Subject(s) - chemistry , tetramer , lactobacillus brevis , flavoprotein , polyethylene glycol , monomer , crystallization , ammonium sulfate , oxidase test , hydrogen peroxide , yield (engineering) , sodium formate , stereochemistry , organic chemistry , enzyme , materials science , bacteria , lactic acid , biology , genetics , lactobacillus plantarum , polymer , metallurgy
NADH oxidase (NOX) from Lactobacillus brevis is a homotetrameric flavoenzyme composed of 450 amino acids per subunit. The molecular weight of each monomer is 48.8 kDa. The enzyme catalyzes the oxidation of two equivalents of NADH and reduces one equivalent of oxygen to yield two equivalents of water, without releasing hydrogen peroxide after the reduction of the first equivalent of NADH. Crystals of this protein were grown in the presence of 34% polyethylene glycol monomethyl ether 2000, 0.1 M sodium acetate and 0.2 M ammonium sulfate at pH 5.4. They belong to the tetragonal space group P 4 3 2 1 2, with unit‐cell parameters a = 74.8, b = 95.7, c = 116.9 Å, α = γ = 90, β = 103.8°. The current diffraction limit is 4.0 Å. The self‐rotation function of the native data set is consistent with a NOX tetramer in the asymmetric unit.