Crystallization and Preliminary Structural Analysis of Dihydrolipoyl Transsuccinylase, the Core of the 2-Oxoglutarate Dehydrogenase Complex

AUTOR(ES)

Derosier, David J.

RESUMO

Dihydrolipoyl transsuccinylase, one of the three enzymes comprising the Escherichia coli 2-oxoglutarate dehydrogenase (EC 1.2.4.2) complex, has been crystallized. Studies by x-ray diffraction and electron microscopy establish that the transsuccinylase has octahedral (432) symmetry, i.e., it consists of 24 subunits that are structurally identical.

Documentos Relacionados

• Genetic characterization of Bacillus subtilis odhA and odhB, encoding 2-oxoglutarate dehydrogenase and dihydrolipoamide transsuccinylase, respectively.
• Sequences directing dihydrolipoamide dehydrogenase (E3) binding are located on the 2-oxoglutarate dehydrogenase (E1) component of the mammalian 2-oxoglutarate dehydrogenase multienzyme complex.
• Structure and regulation of KGD2, the structural gene for yeast dihydrolipoyl transsuccinylase.
• Cloning and nucleotide sequence of the cDNA encoding human 2-oxoglutarate dehydrogenase (lipoamide).
• Crystallization and preliminary X-ray analysis of d-­2-hydroxyacid dehydrogenase from Haloferax mediterranei