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…
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