Crystallization and preliminary analysis of xenobiotic reductase B from Pseudomonas fluorescens I-C.
Single crystals have been obtained of xenobiotic reductase B (XenB), a flavoenzyme isolated and cloned from Pseudomonas fluorescens I-C. The enzyme catalyzes the NADPH-dependent elimination of nitrite from nitroglycerin with an approximately fivefold kinetic preference for the middle nitro group, primarily yielding 1,3-dinitroglycerol. X-ray diffraction data sets have been collected from native crystals to 2.3 A resolution. The space group is P4(1)2(1)2, with unit-cell parameters a = b = 140, c = 95.6 A. The asymmetric unit is likely to contain at least two XenB molecules (V(M) = 3.1 A(3) Da(-1), 60% solvent) and a molecular-replacement solution has been determined in order to solve the structure.
Orville
Allen M
AM
School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332-0400, USA. allen.orville@chemistry.gatech.edu
Manning
Linda
L
Blehert
David S
DS
Fox
Brian G
BG
Chambliss
Glenn H
GH
D003460:Crystallization; D018360:Crystallography, X-Ray; D010088:Oxidoreductases / Q000737:chemistry* / Q000378:metabolism; D011551:Pseudomonas fluorescens / Q000201:enzymology*; D015262:Xenobiotics / Q000378:metabolism*
D015262:Xenobiotics; D010088:Oxidoreductases