1B5S
DIHYDROLIPOYL TRANSACETYLASE (E.C.2.3.1.12) CATALYTIC DOMAIN (RESIDUES 184-425) FROM BACILLUS STEAROTHERMOPHILUS
Summary for 1B5S
| Entry DOI | 10.2210/pdb1b5s/pdb |
| Descriptor | DIHYDROLIPOAMIDE ACETYLTRANSFERASE (1 entity in total) |
| Functional Keywords | dihydrolipoyl transacetylase, pyruvate dehydrogenase, e2p, dihydrolipoyl acetyltransferase, acyltransferase |
| Biological source | Geobacillus stearothermophilus |
| Total number of polymer chains | 5 |
| Total formula weight | 132183.92 |
| Authors | Izard, T.,Aevarsson, A.,Allen, M.D.,Westphal, A.H.,Perham, R.N.,De Kok, A.,Hol, W.G. (deposition date: 1999-01-10, release date: 1999-02-16, Last modification date: 2024-05-22) |
| Primary citation | Izard, T.,Aevarsson, A.,Allen, M.D.,Westphal, A.H.,Perham, R.N.,de Kok, A.,Hol, W.G. Principles of quasi-equivalence and Euclidean geometry govern the assembly of cubic and dodecahedral cores of pyruvate dehydrogenase complexes. Proc.Natl.Acad.Sci.USA, 96:1240-1245, 1999 Cited by PubMed 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. PubMed: 9990008DOI: 10.1073/pnas.96.4.1240 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (4.4 Å) |
Structure validation
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