The multisubunit active site of fumarase C from escherichia coli.
The crystal structure of the tetrameric enzyme, fumarase C from Escherichia coli, has been determined to a resolution of 2.0 Angstroms. 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.
- Research Organization:
- Argonne National Laboratory (ANL)
- Sponsoring Organization:
- ER
- DOE Contract Number:
- AC02-06CH11357
- OSTI ID:
- 937801
- Report Number(s):
- ANL/ER/JA-20342
- Journal Information:
- Nature Struct. Biol., Journal Name: Nature Struct. Biol. Journal Issue: 8 ; Aug. 1995 Vol. 2
- Country of Publication:
- United States
- Language:
- ENGLISH
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