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| - | [[Image:1rqr.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1rqr| PDB=1rqr | SCENE= }} | | {{STRUCTURE_1rqr| PDB=1rqr | SCENE= }} |
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| - | '''Crystal structure and mechanism of a bacterial fluorinating enzyme, product complex'''
| + | ===Crystal structure and mechanism of a bacterial fluorinating enzyme, product complex=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_14765200}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 14765200 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_14765200}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Central 7 stranded beta sheet]] | | [[Category: Central 7 stranded beta sheet]] |
| | [[Category: Fluorinase]] | | [[Category: Fluorinase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:48:16 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:28:52 2008'' |
Revision as of 14:28, 28 July 2008
Template:STRUCTURE 1rqr
Crystal structure and mechanism of a bacterial fluorinating enzyme, product complex
Template:ABSTRACT PUBMED 14765200
About this Structure
1RQR is a Single protein structure of sequence from Streptomyces cattleya. 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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