Crystallization and Preliminary Structural Analysis of Dihydrolipoyl Transsuccinylase, the Core of the 2-Oxoglutarate Dehydrogenase Complex
- 1 June 1971
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 68 (6) , 1135-1137
- https://doi.org/10.1073/pnas.68.6.1135
Abstract
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.Keywords
This publication has 5 references indexed in Scilit:
- Micro diffusion cells for the growth of single protein crystals by means of equilibrium dialysisArchives of Biochemistry and Biophysics, 1968
- The multienzyme alpha-keto acid dehydrogenase complexes.1968
- ALPHA-KETO ACID DEHYDROGENASE COMPLEXES .6. DISSOCIATION AND RECONSTITUTION OF DIHYDROLIPOYL TRANSACETYLASE OF ESCHERICHIA COLI1967
- ALPHA-KETO ACID DEHYDROGENASE COMPLEXES .7. ISOLATION AND PARTIAL CHARACTERIZATION OF POLYPEPTIDE CHAINS IN DIHYDROLIPOYL TRANSACETYLASE OF ESCHERICHIA COLI1967
- RESOLUTION AND RECONSTITUTION OF THE ESCHERICHIA COLI ALPHA-KETOGLUTARATE DEHYDROGENASE COMPLEX.1965