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

Dong, Changjiang, Deng, Hai, Dorward, Mark, Schaffrath, Christoph, O'Hagan, David and Naismith, James H (2003) Crystallization and X-ray diffraction of 5'-fluoro-5'-deoxyadenosine synthase, a fluorination enzyme from Streptomyces cattleya. Acta Crystallographica Section D: Biological Crystallography, 59. pp. 2292-2293. ISSN 0907-4449

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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.

Item Type:	Article
Uncontrolled Keywords:	bacterial proteins,crystallization,crystallography, x-ray,fluorides,pentosyltransferases,protein structure, quaternary,streptomyces
Faculty \ School:	Faculty of Medicine and Health Sciences > Norwich Medical School
UEA Research Groups:	Faculty of Medicine and Health Sciences > Research Groups > Gastroenterology and Gut Biology
Depositing User:	Pure Connector
Date Deposited:	17 Nov 2014 12:56
Last Modified:	08 Mar 2024 00:50
URI:	https://ueaeprints.uea.ac.uk/id/eprint/50993
DOI:	10.1107/S0907444903019826

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