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Science 20 March 1992:
Vol. 255. no. 5051, pp. 1544 - 1550
DOI: 10.1126/science.1549782
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Articles

Science, Vol 255, Issue 5051, 1544-1550
Copyright © 1992 by American Association for the Advancement of Science

articles

Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex

A Mattevi, G Obmolova, E Schulze, KH Kalk, AH Westphal, A de Kok, and WG Hol

Department of Chemistry, University of Groningen, The Netherlands.

The highly symmetric pyruvate dehydrogenase multienzyme complexes have molecular masses ranging from 5 to 10 million daltons. They consist of numerous copies of three different enzymes: pyruvate dehydrogenase, dihydrolipoyl transacetylase, and lipoamide dehydrogenase. The three-dimensional crystal structure of the catalytic domain of Azotobacter vinelandii dihydrolipoyl transacetylase has been determined at 2.6 angstrom (A) resolution. Eight trimers assemble as a hollow truncated cube with an edge of 125 A, forming the core of the multienzyme complex. Coenzyme A must enter the 29 A long active site channel from the inside of the cube, and lipoamide must enter from the outside. The trimer of the catalytic domain of dihydrolipoyl transacetylase has a topology identical to chloramphenicol acetyl transferase. The atomic structure of the 24-subunit cube core provides a framework for understanding all pyruvate dehydrogenase and related multienzyme complexes.


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