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

Changjiang Dong, Hai Deng, Mark Dorward, Christoph Schaffrath, David O'Hagan, James H Naismith

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)

Abstract

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 A, alpha = beta = gamma = 90 degrees. Data were recorded to 1.9 A at the ESRF. The structure of the protein should provide important insights into the biochemical process of C-F bond formation.
Original languageEnglish
Pages (from-to)2292-2293
Number of pages2
JournalActa Crystallographica Section D: Biological Crystallography
Volume59
DOIs
Publication statusPublished - Dec 2003

Keywords

  • Bacterial Proteins
  • Crystallization
  • Crystallography, X-Ray
  • Fluorides
  • Pentosyltransferases
  • Protein Structure, Quaternary
  • Streptomyces

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