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Crystallization and X-ray diffraction of 5 '-fluoro-5 '-deoxyadenosine synthase, a fluorination enzyme from Streptomyces cattleya

Author(s): C. J. Dong, H. Deng, M. Dorward, C. Schaffrath, D. O'Hagan, J. H. Naismith

Organofluorine compounds are widely prepared throughout the chemicals industry, but their prepararion generally requires harsh fluorinating reagents and non-aqueous solvents. On the other hand, biology has hardly exploited organofluorine compounds. A very few organisms synthesize organofluorine metabolites, suggesting they have evolved a mechanism to overcome the kinetic desolvation barrier to utilizing F-(aq). Here, the purification and crystallization of an enzyme from Streptomyces cattleya which is responsible for the synthesis of the C-F bond during fluoroacetate and 4-fluorothreonine biosynthesis is reported. The protein crystallizes in space group C222(1), with unit-cell parameters a = 75.9, b = 130.3, c = 183.4 Angstrom, alpha = beta = gamma = 90degrees. Data were recorded to 1.9 Angstrom at the ESRF. The structure of the protein should provide important insights into the biochemical process of C-F bond formation.

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ISBN: 0907-4449
Publication Year: 2003
Periodical: Acta Crystallographica Section D-Biological Crystallography
Periodical Number:
Volume: 59
Pages: 2292-2293
Author Address: