1rqr

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spinqualitylabelsall models 1rqr, resolution 2.67Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure and mechanism of a bacterial fluorinating enzyme, product complex

Overview

Fluorine is the thirteenth most abundant element in the earth's crust, but, fluoride concentrations in surface water are low and fluorinated, metabolites are extremely rare. The fluoride ion is a potent nucleophile, in its desolvated state, but is tightly hydrated in water and effectively, inert. Low availability and a lack of chemical reactivity have largely, excluded fluoride from biochemistry: in particular, fluorine's high redox, potential precludes the haloperoxidase-type mechanism used in the, metabolic incorporation of chloride and bromide ions. But fluorinated, chemicals are growing in industrial importance, with applications in, pharmaceuticals, agrochemicals and materials products. Reactive, fluorination reagents requiring specialist process technologies are needed, in industry and, although biological catalysts for these processes are, highly sought after, only one enzyme that can convert fluoride to organic, fluorine has been described. Streptomyces cattleya can form, carbon-fluorine bonds and must therefore have evolved an enzyme able to, overcome the chemical challenges of using aqueous fluoride. Here we report, the sequence and three-dimensional structure of the first native, fluorination enzyme, 5'-fluoro-5'-deoxyadenosine synthase, from this, organism. Both substrate and products have been observed bound to the, enzyme, enabling us to propose a nucleophilic substitution mechanism for, this biological fluorination reaction.

About this Structure

1RQR is a Single protein structure of sequence from Streptomyces cattleya with 5FD and MET as ligands. Active as Adenosyl-fluoride synthase, with EC number 2.5.1.63 Full crystallographic information is available from OCA.

Reference

Crystal structure and mechanism of a bacterial fluorinating enzyme., Dong C, Huang F, Deng H, Schaffrath C, Spencer JB, O'Hagan D, Naismith JH, Nature. 2004 Feb 5;427(6974):561-5. PMID:14765200

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