1EBD

DIHYDROLIPOAMIDE DEHYDROGENASE COMPLEXED WITH THE BINDING DOMAIN OF THE DIHYDROLIPOAMIDE ACETYLASE

Summary for 1EBD

• Entry DOI: 10.2210/pdb1ebd/pdb
• Descriptor: DIHYDROLIPOAMIDE DEHYDROGENASE, DIHYDROLIPOAMIDE ACETYLTRANSFERASE, FLAVIN-ADENINE DINUCLEOTIDE, ... (4 entities in total)
• Functional Keywords: redox-active center, glycolysis, oxidoreductase, complex (oxidoreductase-transferase) complex, complex (oxidoreductase/transferase)
• Biological source: Geobacillus stearothermophilus; More
• Cellular location: Cytoplasm: P11959
• Total number of polymer chains: 3
• Total formula weight: 101600.13

Authors

Mande, S.S.,Sarfaty, S.,Allen, M.D.,Perham, R.N.,Hol, W.G.J. (deposition date: 1996-02-03, release date: 1996-07-11, Last modification date: 2024-10-23)

Primary citation

Mande, S.S.,Sarfaty, S.,Allen, M.D.,Perham, R.N.,Hol, W.G.
Protein-protein interactions in the pyruvate dehydrogenase multienzyme complex: dihydrolipoamide dehydrogenase complexed with the binding domain of dihydrolipoamide acetyltransferase.
Structure, 4:277-286, 1996

PubMed Abstract: The ubiquitous pyruvate dehydrogenase multienzyme complex is built around an octahedral or icosahedral core of dihydrolipoamide acetyltransferase (E2) chains, to which multiple copies of pyruvate decarboxylase (E1) and dihydrolipoamide dehydrogenase (E3) bind tightly but non-covalently. E2 is a flexible multidomain protein that mediates interactions with E1 and E3 through a remarkably small binding domain (E2BD).

PubMed: 8805537
DOI: 10.1016/S0969-2126(96)00032-9

Experimental method

X-RAY DIFFRACTION (2.6 Å)