In:
Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 96, No. 4 ( 1999-02-16), p. 1240-1245
Abstract:
The pyruvate dehydrogenase multienzyme complex
( M r 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 ≈237 Å, 12 large openings of ≈52 Å diameter across the fivefold axes, and an inner
cavity with a diameter of ≈118 Å. 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.
Type of Medium:
Online Resource
ISSN:
0027-8424
,
1091-6490
DOI:
10.1073/pnas.96.4.1240
Language:
English
Publisher:
Proceedings of the National Academy of Sciences
Publication Date:
1999
detail.hit.zdb_id:
209104-5
detail.hit.zdb_id:
1461794-8
SSG:
11
SSG:
12
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