Subunit composition, crystallization and preliminary crystallographic studies of the Desulfovibrio gigas aldehyde oxidoreductase containing molybdenum and [2Fe-2S] centers.
The Desulfovibrio gigas aldehyde oxidoreductase contains molybdenum bound to a pterin cofactor and [2Fe-2S] centers. The enzyme was characterized by SDS/PAGE, gel-filtration and analytical ultracentrifugation experiments. It was crystallized at 4 degrees C, pH 7.2, using isopropanol and MgCl2 as precipitants. The crystals diffract beyond 0.3-nm (3.0-A) resolution and belong to space group P6(1)22 or its enantiomorph, with cell dimensions a = b = 14.45 nm and c = 16.32 nm. There is one subunit/asymmetric unit which gives a packing density of 2.5 x 10(-3) nm3/Da (2.5 A3/Da), consistent with the experimental crystal density, rho = 1.14 g/cm3. One dimer (approximately 2 x 100 kDa) is located on a crystallographic twofold axis.
Romão
M J
MJ
Istituto de Tecnologia Química e Biológica, Oeiras, Portugal.
Barata
B A
BA
Archer
M
M
Lobeck
K
K
Moura
I
I
Carrondo
M A
MA
LeGall
J
J
Lottspeich
F
F
Huber
R
R
Moura
J J
JJ
D000445:Aldehyde Oxidoreductases / Q000737:chemistry*; D000595:Amino Acid Sequence; D003460:Crystallization; D003901:Desulfovibrio / Q000201:enzymology*; D007506:Iron-Sulfur Proteins / Q000032:analysis*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D008982:Molybdenum / Q000032:analysis*; D014961:X-Ray Diffraction
D007506:Iron-Sulfur Proteins; D008982:Molybdenum; D000445:Aldehyde Oxidoreductases