1RQP
Crystal structure and mechanism of a bacterial fluorinating enzyme
Summary for 1RQP
| Entry DOI | 10.2210/pdb1rqp/pdb |
| Descriptor | 5'-fluoro-5'-deoxyadenosine synthase, S-ADENOSYLMETHIONINE (3 entities in total) |
| Functional Keywords | fluorinase, central 7 stranded beta sheets, anti-parallel beta sheets, transferase |
| Biological source | Streptomyces cattleya |
| Total number of polymer chains | 3 |
| Total formula weight | 98399.78 |
| Authors | Dong, C.,Huang, F.,Deng, H.,Schaffrath, C.,Spencer, J.B.,O'Hagan, D.,Naismith, J.H. (deposition date: 2003-12-06, release date: 2004-03-02, Last modification date: 2024-02-14) |
| Primary citation | Dong, C.,Huang, F.,Deng, H.,Schaffrath, C.,Spencer, J.B.,O'Hagan, D.,Naismith, J.H. Crystal structure and mechanism of a bacterial fluorinating enzyme Nature, 427:561-565, 2004 Cited by PubMed Abstract: 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. PubMed: 14765200DOI: 10.1038/nature02280 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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