Mobility in pyruvate dehydrogenase complexes with multiple lipoyl domains
- 1 June 1993
- journal article
- Published by Wiley in FEBS Letters
- Vol. 323 (3) , 243-246
- https://doi.org/10.1016/0014-5793(93)81349-5
Abstract
High-field NMR studies were carried out with genetically-reconstructed pyruvate dehydrogenase (PDH) complexes of Escherichia coli containing from zero to nine lipoyl domains per lipoate acetyltransferase (E2p) subunit. The only significant differences between the NMR spectra were the increasing intensities of the signals derived from the lipoyl domains and their associated linkers, and the much enhanced signal from the E3-binding domain and its linker in complexes that are devoid of lipoyl domains. The results suggest an explanation for the presence of three lipoyl domains per E2p subunit in the wild-type PDH complex, based on its greater inherent mobility, and potentially more efficient active-site coupling, than any of the other complexes.Keywords
This publication has 16 references indexed in Scilit:
- Restructuring an interdomain linker in the dihydrolipoamide acetyltransferase component of the pyruvate dehydrogenase complex of Escherichia coliProtein Engineering, Design and Selection, 1993
- Construction and properties of pyruvate dehydrogenase complexes with up to nine lipoyl domains per lipoate acetyltransferase chainFEMS Microbiology Letters, 1992
- Construction and properties of pyruvate dehydrogenase complexes with up to nine lipoyl domains per lipoate acetyltransferase chainFEMS Microbiology Letters, 1992
- Configuration of interdomain linkers in pyruvate dehydrogenase complex of Escherichia coli as determined by cryoelectron microscopyJournal of Structural Biology, 1992
- Atomic Structure of the Cubic Core of the Pyruvate Dehydrogenase Multienzyme EomplexScience, 1992
- Domains, motifs, and linkers in 2-oxo acid dehydrogenase multienzyme complexes: a paradigm in the design of a multifunctional proteinBiochemistry, 1991
- Sequence similarities within the family of dihydrolipoamide acyltransferases and discovery of a previously unidentified fungal enzymeBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1991
- Structure, Expression, and Protein Engineering of the Pyruvate Dehydrogenase Complex of Escherichia coliaAnnals of the New York Academy of Sciences, 1989
- Investigation of the mechanism of active site coupling in the pyruvate dehydrogenase multienzyme complex of Escherichia coli by protein engineeringJournal of Molecular Biology, 1988
- Genetic reconstruction and functional analysis of the repeating lipoyl domains in the pyruvate dehydrogenase multienzyme complex of Escherichia coliJournal of Molecular Biology, 1985