Principles of quasi-equivalence and Euclidean geometry govern the assembly of cubic and dodecahedral cores of pyruvate dehydrogenase complexes
Year: 1999
Type: article
Abstract: The pyruvate dehydrogenase multienzyme complex (Mr of 5-10 million) is assembled around a structural core formed of multiple copies of dihydrolipoyl acetyltransferase (E2p), which exhibits the shape of either a cube or a dodecahedron, depending on the source. The crystal structures of the 60-meric dihydrolipoyl acyltransferase cores of Bacillus stearothermophilus and Enterococcus faecalis pyruvate dehydrogenase complexes were determined and revealed a remarkably hollow dodecahedron with an outer diameter of approximately 237 A, 12 large openings of approximately 52 A diameter across the fivefold axes, and an inner cavity with a diameter of approximately 118 A. Comparison of cubic and dodecahedral E2p assemblies shows that combining the principles of quasi-equivalence formulated by Caspar and Klug [Caspar, D. L. & Klug, A. (1962) Cold Spring Harbor Symp. Quant. Biol. 27, 1-4] with strict Euclidean geometric considerations results in predictions of the major features of the E2p dodecahedron matching the observed features almost exactly.
Language: English
Subfield: Biochemistry
Domain: Life Sciences
Open Access status: green
Funders: M.J. Murdock Charitable Trust, Wellcome Trust, European Molecular Biology Laboratory, Swedish Foundation for International Cooperation in Research and Higher Education, Nederlandse Organisatie voor Wetenschappelijk Onderzoek, Directorate for Biological Sciences, Biotechnology and Biological Sciences Research Council
OpenAlex ID: W2120842521