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- Title
Prediction of the binding site on E1 in the assembly of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus
- Authors
Jung, Hyo-Il; Perham, Richard N.
- Abstract
The β-subunit (E1β) of the pyruvate decarboxylase (E1, α2β2) component of the Bacillus stearothermophilus pyruvate dehydrogenase complex was comparatively modelled based on the crystal structures of the homologous 2-oxoisovalerate decarboxylase of Pseudomonas putida and Homo sapiens. Based on this homology modelling, alanine-scanning mutagenesis studies revealed that the negatively charged side chain of Glu285 and the hydrophobic side chain of Phe324 are of particular importance in the interaction with the peripheral subunit-binding domain of the dihydrolipoyl acetyltransferase component of the complex. These results help to identify the site of interaction on the E1β subunit and are consistent with thermodynamic evidence of a mixture of electrostatic and hydrophobic interactions being involved.
- Subjects
PYRUVATE carboxylase; SURFACE plasmon resonance; DEHYDROGENASES; ALANINE
- Publication
FEBS Letters, 2003, Vol 555, Issue 2, p405
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/S0014-5793(03)01245-6