Crystallization of mouse lung carbonyl reductase complexed with NADPH and analysis of symmetry of its tetrameric molecule.
Mouse lung carbonyl reductase (MLCR), which belongs to the short-chain dehydrogenase/reductase family, is an oxidoreductase involved in the metabolism of biogenic and xenobiotic carbonyl compounds. The crystals of MLCR complexed with its cofactor NADPH belong to a monoclinic space group P2(1) with dimensions a = 79.73 A, b = 105.5 A, c = 60.87 A, and beta = 91.43 degrees. X-ray diffraction data were collected up to 1.8 A resolution using a macromolecule-oriented Weissenberg camera at the Photon Factory synchrotron radiation source. Studies using a self-rotation function revealed the presence of a twofold rotational symmetry relating the subunits. This suggests that the tetrameric MLCR molecule has the 222 point group symmetry.
Tanaka
N
N
Department of BioEngineering, Nagaoka University of Technology, Kamitomioka.
Nonaka
T
T
Nakanishi
M
M
Deyashiki
Y
Y
Hara
A
A
D000429:Alcohol Oxidoreductases / Q000737:chemistry*; D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D008168:Lung / Q000201:enzymology*; D051379:Mice; D009249:NADP / Q000737:chemistry*; D011487:Protein Conformation; D012399:Rotation
D009249:NADP; D000429:Alcohol Oxidoreductases