The multisubunit active site of fumarase C from Escherichia coli

@article{Weaver1995TheMA,
  title={The multisubunit active site of fumarase C from Escherichia coli},
  author={Todd M. Weaver and David G. Levitt and Mark Donnelly and P. P. Wilkens Stevens and Leonard J. Banaszak},
  journal={Nature Structural Biology},
  year={1995},
  volume={2},
  pages={654-662}
}
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… CONTINUE READING

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