The multisubunit active site of fumarase c from escherichia coli

T. M. Weaver, David G Levitt, M. I. Donnelly, P. P. Wilkens Stevens, L. J. Banaszak

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

Original languageEnglish (US)
Pages (from-to)654-662
Number of pages9
JournalNature Structural Biology
Issue number8
StatePublished - Aug 1995


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