The multisubunit active site of fumarase C from Escherichia coli

Nat Struct Biol. 1995 Aug;2(8):654-62. doi: 10.1038/nsb0895-654.


The crystal structure of the tetrameric enzyme, fumarase C from Escherichia coli, has been determined to a resolution of 2.0 A. A tungstate derivative used in the X-ray analysis is a competitive inhibitor and places the active site of fumarase in a region which includes atoms from three of the four subunits. The polypeptide conformation is similar to that of delta-crystallin and is comprised of three domains. The central domain, D2, is a unique five-helix bundle. The association of the D2 domains results in a tetramer which has a core of 20 alpha-helices. The other two domains, D1 and D3, cap the helical bundle on opposite ends giving both the single subunit and the tetramer a dumbbell-like appearance. Fumarase C has sequence homology to the eukaryotic fumarases, aspartase, arginosuccinate lyase, adenylosuccinate lyase and delta-crystallin.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Adenylosuccinate Lyase / chemistry
  • Amino Acid Sequence
  • Argininosuccinate Lyase / chemistry
  • Aspartate Ammonia-Lyase / chemistry
  • Base Sequence
  • Binding Sites
  • Computer Simulation
  • Crystallins / chemistry
  • Crystallography, X-Ray
  • DNA Primers
  • Escherichia coli / enzymology*
  • Escherichia coli / genetics
  • Fumarate Hydratase / chemistry*
  • Fumarate Hydratase / metabolism
  • Genes, Bacterial
  • Kinetics
  • Macromolecular Substances
  • Models, Molecular
  • Molecular Sequence Data
  • Polymerase Chain Reaction
  • Protein Structure, Secondary*
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Sequence Homology, Amino Acid


  • Crystallins
  • DNA Primers
  • Macromolecular Substances
  • Recombinant Proteins
  • fumarase C
  • Fumarate Hydratase
  • Aspartate Ammonia-Lyase
  • Argininosuccinate Lyase
  • Adenylosuccinate Lyase