Crystal structure of eucaryotic E3, lipoamide dehydrogenase from yeast
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Toyoda, T
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机构:Tokyo Inst Technol, Fac Biosci & Biotechnol, Dept Life Sci, Yokohama, Kanagawa 2268501, Japan
Toyoda, T
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Suzuki, K
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Sekiguchi, T
Reed, LJ
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机构:Tokyo Inst Technol, Fac Biosci & Biotechnol, Dept Life Sci, Yokohama, Kanagawa 2268501, Japan
Reed, LJ
Takenaka, A
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Tokyo Inst Technol, Fac Biosci & Biotechnol, Dept Life Sci, Yokohama, Kanagawa 2268501, JapanTokyo Inst Technol, Fac Biosci & Biotechnol, Dept Life Sci, Yokohama, Kanagawa 2268501, Japan
Takenaka, A
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[1] Tokyo Inst Technol, Fac Biosci & Biotechnol, Dept Life Sci, Yokohama, Kanagawa 2268501, Japan
[2] Iwaki Meisei Univ, Fac Sci & Technol, Dept Fundamental Sci, Fukushima 9708551, Japan
[3] Univ Texas, Inst Biochem, Austin, TX 78712 USA
The crystal structure of eucaryotic lipoamide dehydrogenase from yeast has been determined by an X-ray analysis at 2.7 (partially at 2.4) Angstrom resolution, The enzyme has two identical subunits related by a pseudo twofold symmetry. The tertiary structure is similar to those of other procaryotic enzymes, The active site, consisting of FAD, Cys44, and Cys49 from one subunit and His457' from the other subunit, is highly conserved, This enzyme is directly bound to the core protein E2 of the 2-oxoglutarate dehydrogenase complex, whereas it is bound to the pyruvate dehydrogenase complex through a protein X. The calculated electrostatic potential suggests two characteristic regions for binding with these two proteins.