1jeh

CRYSTAL STRUCTURE OF YEAST E3, LIPOAMIDE DEHYDROGENASE

spinqualitylabelsall models 1jeh, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1jeh is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FAD Activity: Dihydrolipoyl dehydrogenase, with EC number 1.8.1.4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [DLDH_YEAST] Lipoamide dehydrogenase is a component of the alpha-ketoacid dehydrogenase complexes. This includes the pyruvate dehydrogenase complex, which catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). Acts also as component of the glycine cleavage system (glycine decarboxylase complex), which catalyzes the degradation of glycine. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Crystal structure of eucaryotic E3, lipoamide dehydrogenase from yeast.,Toyoda T, Suzuki K, Sekiguchi T, Reed LJ, Takenaka A J Biochem. 1998 Apr;123(4):668-74. PMID:9538259 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Dihydrolipoamide dehydrogenase

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