FEBS Letters | |
Prediction of the binding site on E1 in the assembly of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus | |
Perham, Richard N1  Jung, Hyo-Il1  | |
[1] Cambridge Centre for Molecular Recognition, Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, UK | |
关键词: Pyruvate dehydrogenase; Homology modelling; Multienzyme complex; Alanine-scanning mutagenesis; Protein–protein interaction; PDH; pyruvate dehydrogenase; BCDH; branched-chain 2-oxo acid dehydrogenase; E1; pyruvate decarboxylase (EC 1.2.4.1); E2; dihydrolipoyl acetyltransferase (EC 2.3.1.12); E3; dihydrolipoyl dehydrogenase (EC 1.8.1.4); PSBD; peripheral subunit-binding domain; LD; lipoyl domain; CD; catalytic domain; ThDD; thrombin-cleavable di-domain; SPR; surface plasmon resonance; | |
DOI : 10.1016/S0014-5793(03)01245-6 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
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.
【 授权许可】
Unknown
【 预 览 】
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