1b5s

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Revision as of 09:16, 20 November 2007

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spinqualitylabelsall models 1b5s, resolution 4.4Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

DIHYDROLIPOYL TRANSACETYLASE (E.C.2.3.1.12) CATALYTIC DOMAIN (RESIDUES 184-425) FROM BACILLUS STEAROTHERMOPHILUS

Overview

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.

About this Structure

1B5S is a Single protein structure of sequence from Geobacillus stearothermophilus. Active as Dihydrolipoyllysine-residue acetyltransferase, with EC number 2.3.1.12 Full crystallographic information is available from OCA.

Reference

Principles of quasi-equivalence and Euclidean geometry govern the assembly of cubic and dodecahedral cores of pyruvate dehydrogenase complexes., Izard T, Aevarsson A, Allen MD, Westphal AH, Perham RN, de Kok A, Hol WG, Proc Natl Acad Sci U S A. 1999 Feb 16;96(4):1240-5. PMID:9990008

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