ATOMIC-STRUCTURE OF THE CUBIC CORE OF THE PYRUVATE-DEHYDROGENASE MULTIENZYME COMPLEX

A MATTEVI, G OBMOLOVA, E SCHULZE, KH KALK, AH WESTPHAL, A DEKOK, WGJ HOL

Research output: Contribution to journalArticleAcademicpeer-review

208 Citations (Scopus)

Abstract

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 (angstrom) resolution. Eight trimers assemble as a hollow truncated cube with an edge of 125 angstrom, forming the core of the multienzyme complex. Coenzyme A must enter the 29 angstrom 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 cubic core provides a framework for understanding all pyruvate dehydrogenase and related multienzyme complexes.

Original languageEnglish
Pages (from-to)1544-1550
Number of pages7
JournalScience
Volume255
Issue number5051
Publication statusPublished - 20-Mar-1992

Keywords

  • DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT
  • ESCHERICHIA-COLI
  • CHLORAMPHENICOL ACETYLTRANSFERASE
  • NUCLEOTIDE-SEQUENCE
  • SUBUNIT STRUCTURE
  • SITE
  • MECHANISM
  • CRYSTALLIZATION
  • OVEREXPRESSION
  • MUTAGENESIS

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