Binding of pyruvate dehydrogenase to the core of the human pyruvate dehydrogenase complex

• Published in: FEBS letters 2008-02, Vol.582 (3), p.468-472
• Main Authors: Korotchkina, Lioubov G., Patel, Mulchand S.
• Format: Article
• Language: English
• Subjects: 2,6-dichlorophenolindophenol; Bacillus stearothermophilus; Binding Sites; DCPIP; dihydrolipoamide acetyltransferase; E3, dihydrolipoamide dehydrogenase; E3-binding protein; fragment containing the second lipoyl domain (L2), the second hinge region, the E1-binding domain and the third hinge region of human E2; Humans; Ketone Oxidoreductases - metabolism; L2S; Models, Molecular; Mutagenesis, Site-Directed; Mutant Proteins - metabolism; PDC; Protein Binding; Protein Structure, Tertiary; pyruvate dehydrogenase; pyruvate dehydrogenase complex; Pyruvate Dehydrogenase Complex - chemistry; Pyruvate Dehydrogenase Complex - genetics; Pyruvate Dehydrogenase Complex - metabolism; SPR; Substrate Specificity; Subunit-binding domain; Subunit–subunit interaction; Surface plasmon resonance
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/j.febslet.2007.12.041

In human (h) pyruvate dehydrogenase complex (PDC) the pyruvate dehydrogenase (E1) is bound to the E1-binding domain of dihydrolipoamide acetyltransferase (E2). The C-terminal surface of the E1β subunit was scanned for the negatively charged residues involved in binding with E2. βD289 of hE1 interacts with K276 of hE2 in a manner similar to the corresponding interaction in Bacillus stearothermophilus PDC. In contrast to bacterial E1β, the C-terminal residue of the hE1β does not participate in the binding with positively charged residues of hE2. This latter finding shows species specificity in the interaction between hE1β and hE2 in PDC.