Crystallization and X-ray diffraction of 5'-fluoro-5'-deoxyadenosine synthase, a fluorination enzyme from Streptomyces cattleya.
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.
Dong
Changjiang
C
Centre for Biomolecular Sciences, University of St Andrews, North Haugh, St Andrews, Fife KY16 9ST, Scotland.
Deng
Hai
H
Dorward
Mark
M
Schaffrath
Christoph
C
O'Hagan
David
D
Naismith
James H
JH
D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D005459:Fluorides / Q000378:metabolism; D010430:Pentosyltransferases / Q000737:chemistry* / Q000302:isolation & purification; D020836:Protein Structure, Quaternary; D013302:Streptomyces / Q000201:enzymology*
D001426:Bacterial Proteins; C477004:5'-fluorodeoxyadenosine synthase; D010430:Pentosyltransferases; D005459:Fluorides