Crystallization of Mouse Lung Carbonyl Reductase Complexed with NADPH and Analysis of Symmetry of Its Tetrameric Molecule.
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概要
- 論文の詳細を見る
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 P21 with dimensions a=79.73 Å, b=105.5 Å, c=60.87 Å, and β=91.43°. X-Ray diffraction data were collected up to 1.8 Å 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.
- 社団法人 日本生化学会の論文
著者
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Nonaka Takamasa
Department Of Bioengineering Nagaoka University Of Technology
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MITSUI Yukio
Department of BioEngineering Nagaoka University of Technology
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Tanaka Nobutada
Department Of Applied Chemistry Kyushu Institute Of Technology
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Hara Akira
Laboratory Of Biochemistry And Nutritional Chemistry:(present Address)faculty Of Agriculture Meijo U
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Deyashiki Yoshihiro
Laboratory Of Biochemistry Gifu Pharmaceutical University
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Nakanishi Masayuki
Laboratory of Biochemistry, Gifu Pharmaceutical University
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