Crystal structure of eucaryotic E3, lipoamide dehydrogenase from yeast

Journal of Biochemistry
T ToyodaA Takenaka

Abstract

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.

Citations

Sep 7, 2000·Current Opinion in Biotechnology·A W MunroM D Walkinshaw
Feb 15, 2000·Annals of the New York Academy of Sciences·K F Sheu, J P Blass
May 9, 2006·The Journal of Biological Chemistry·Michaela SmolleJohn Gordon Lindsay
Aug 17, 1999·Biochemical and Biophysical Research Communications·E ShanyO N Elpeleg

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