Crystallization of Mouse Lung Carbonyl Reductase Complexed with NADPH and Analysis of Symmetry of Its Tetrameric Molecule1

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, with dimensions a = 79.73 A, 6 = 105.5 A, c =60.87 A, and #=91.43°. 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. Key words: adipocyte 27-kDa protein, self-rotation search, short-chain dehydrogenase/ reductase family, tetrameric enzyme, X-ray crystal structure analysis. Mammalian lung carbonyl reductases [EC 1.1.1.184] are oxidoreductases involved in the metabolism of biogenic and xenobiotic carbonyl compounds. They were isolated and purified from the lungs of guinea pig, mouse, and pig (1-3)