1JEH
CRYSTAL STRUCTURE OF YEAST E3, LIPOAMIDE DEHYDROGENASE
Summary for 1JEH
| Entry DOI | 10.2210/pdb1jeh/pdb |
| Descriptor | DIHYDROLIPOAMIDE DEHYDROGENASE, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total) |
| Functional Keywords | 2-oxoglutarate dehydrogenase complex, pyruvate dehydrogenase complex, oxidoreductase |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Total number of polymer chains | 2 |
| Total formula weight | 104819.08 |
| Authors | Toyoda, T.,Suzuki, K.,Sekigushi, T.,Reed, J.,Takenaka, A. (deposition date: 2001-06-18, release date: 2001-07-11, Last modification date: 2023-10-25) |
| Primary citation | Toyoda, T.,Suzuki, K.,Sekiguchi, T.,Reed, L.J.,Takenaka, A. Crystal structure of eucaryotic E3, lipoamide dehydrogenase from yeast. J.Biochem., 123:668-674, 1998 Cited by PubMed 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. PubMed: 9538259DOI: 10.1093/oxfordjournals.jbchem.a021989 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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