Crystal structure of eucaryotic E3, lipoamide dehydrogenase from yeast.
The crystal structure of eucaryotic lipoamide dehydrogenase from yeast has been determined by an X-ray analysis at 2.7 (partially at 2.4) A 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.
Toyoda
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Department of Life Science, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama 226-8501.
Suzuki
K
K
Sekiguchi
T
T
Reed
L J
LJ
Takenaka
A
A
D000595:Amino Acid Sequence; D000818:Animals; D018360:Crystallography, X-Ray; D008058:Dihydrolipoamide Dehydrogenase / Q000737:chemistry*; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D017386:Sequence Homology, Amino Acid; D055672:Static Electricity
D008058:Dihydrolipoamide Dehydrogenase