The multisubunit active site of fumarase C from Escherichia coli

Author: Weaver, T. M.; Levitt, D. G.; Donnelly, M. I.; Stevens, P. P.; Banaszak, L. J.

Description: 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.

Subject headings: Adenylosuccinate Lyase; Amino Acid Sequence; Argininosuccinate Lyase; Aspartate Ammonia-Lyase; Base Sequence; Binding Sites; Computer Simulation; Crystallins; Crystallography; X-Ray; DNA Primers; Escherichia coli; Fumarate Hydratase; Genes; Bacterial; Kinetics; Macromolecular Substances; Models; Molecular; Molecular Sequence Data; Polymerase Chain Reaction; Protein Structure; Secondary; Recombinant Proteins; Sequence Homology; Amino Acid

Publication year: 1995

Journal or book title: Nature Structural Biology

Volume: 2

Issue: 8

Pages: 654-662

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Serial number: 3931