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The multisubunit active site of fumarase C from Escherichia coli

Nature Structural Biology volume 2, pages 654–662 (1995)Cite this article

Abstract

The crystal structure of the tetrameric enzyme, fumarase C from Escherichia coli, has been determined to a resolution of 2.0 Å. 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 δ-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 α-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 δ-crystallin.

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Authors and Affiliations

  1. Department of Biochemistry, University of Minnesota, Minneapolis, Minnesota, 55455, USA

    T.M. Weaver & L.J. Banaszak

  2. Department of Physiology, University of Minnesota, Minneapolis, Minnesota, 55455, USA

    D.G. Levitt

  3. Environmental Research Division, Argonne National Laboratory, Argonne, Illinois, 60439, USA

    M.I. Donnelly

  4. Center for Mechanistic Biology, Argonne National Laboratory, Argonne, Illinois, 60439, USA

    P.P. Wilkens Stevens

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  4. P.P. Wilkens Stevens
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  5. L.J. Banaszak
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Weaver, T., Levitt, D., Donnelly, M. et al. The multisubunit active site of fumarase C from Escherichia coli. Nat Struct Mol Biol 2, 654–662 (1995). https://doi.org/10.1038/nsb0895-654

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