PMID:7552727
| Citation |
Weaver, TM, Levitt, DG, Donnelly, MI, Stevens, PP and Banaszak, LJ (1995) The multisubunit active site of fumarase C from Escherichia coli. Nat. Struct. Biol. 2:654-62 |
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| Abstract |
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 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. |
| Links | |
| Keywords |
Adenylosuccinate Lyase/chemistry; Amino Acid Sequence; Argininosuccinate Lyase/chemistry; Aspartate Ammonia-Lyase/chemistry; Base Sequence; Binding Sites; Computer Simulation; Crystallins/chemistry; Crystallography, X-Ray; DNA Primers; Escherichia coli/enzymology; Escherichia coli/genetics; Fumarate Hydratase/chemistry; Fumarate Hydratase/metabolism; Genes, Bacterial; Kinetics; Macromolecular Substances; Models, Molecular; Molecular Sequence Data; Polymerase Chain Reaction; Protein Structure, Secondary; Recombinant Proteins/chemistry; Recombinant Proteins/metabolism; Sequence Homology, Amino Acid |
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