Crystallization and preliminary diffraction studies of pentaerythritol tetranitrate reductase from Enterobacter cloacae PB2.
Pentaerythritol tetranitrate (PETN) reductase of Enterobacter cloacae PB2, a flavoprotein involved in the biodegradation of the explosive PETN, ethylene glycol dinitrate (EGDN) and glycerol trinitrate (GTN), was purified from an overexpressing strain of E. coli and crystallized at 293 K using the sitting-drop vapour-diffusion method. Diffraction data can be seen at 1.8 A. The primitive orthorhombic cell has a monomer in the asymmetric unit. Preliminary molecular-replacement calculations have been performed using a search model based on Old Yellow enzyme.
Department of Biochemistry, University of Leicester, Adrian Building, University Road, Leicester LE1 7RH, England. pcem1@le.ac.uk
P C
PC
Moody
N
N
Shikotra
C E
CE
French
N C
NC
Bruce
N S
NS
Scrutton
D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D016972:Enterobacter cloacae / Q000201:enzymology*; D009252:NADPH Dehydrogenase / Q000737:chemistry; D010088:Oxidoreductases / Q000737:chemistry* / Q000302:isolation & purification; D011487:Protein Conformation
D001426:Bacterial Proteins; D010088:Oxidoreductases; D009252:NADPH Dehydrogenase; C098939:pentaerythritol tetranitrate reductase