1rqp

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[[Image:1rqp.gif|left|200px]]
 
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{{Structure
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==Crystal structure and mechanism of a bacterial fluorinating enzyme==
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|PDB= 1rqp |SIZE=350|CAPTION= <scene name='initialview01'>1rqp</scene>, resolution 1.80&Aring;
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<StructureSection load='1rqp' size='340' side='right'caption='[[1rqp]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>
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<table><tr><td colspan='2'>[[1rqp]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_cattleya Streptomyces cattleya]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RQP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RQP FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosyl-fluoride_synthase Adenosyl-fluoride synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.63 2.5.1.63] </span>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rqp OCA], [https://pdbe.org/1rqp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rqp RCSB], [https://www.ebi.ac.uk/pdbsum/1rqp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rqp ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rqp OCA], [http://www.ebi.ac.uk/pdbsum/1rqp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rqp RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/FLA_STRCT FLA_STRCT] Involved in the biosynthesis of fluorometabolites. Catalyzes the formation of a C-F bond by combining S-adenosyl-L-methionine (SAM) and fluoride to generate 5'-fluoro-5'-deoxyadenosine (5'-FDA) and L-methionine. It can also use 2'-deoxyadenosine in place of adenosine as substrate.<ref>PMID:12860396</ref> <ref>PMID:14765200</ref> <ref>PMID:16370017</ref> <ref>PMID:16604208</ref> <ref>PMID:16720268</ref> <ref>PMID:17985882</ref>
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== Evolutionary Conservation ==
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'''Crystal structure and mechanism of a bacterial fluorinating enzyme'''
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rq/1rqp_consurf.spt"</scriptWhenChecked>
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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.
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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==About this Structure==
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</jmolCheckbox>
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1RQP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_cattleya Streptomyces cattleya]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RQP OCA].
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1rqp ConSurf].
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<div style="clear:both"></div>
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==Reference==
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== References ==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/14765200 14765200]
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<references/>
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[[Category: Adenosyl-fluoride synthase]]
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__TOC__
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[[Category: Single protein]]
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Streptomyces cattleya]]
[[Category: Streptomyces cattleya]]
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[[Category: Deng, H.]]
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[[Category: Deng H]]
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[[Category: Dong, C.]]
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[[Category: Dong C]]
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[[Category: Hagan, D O.]]
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[[Category: Huang F]]
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[[Category: Huang, F.]]
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[[Category: Naismith JH]]
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[[Category: Naismith, J H.]]
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[[Category: O'Hagan D]]
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[[Category: Schaffrath, C.]]
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[[Category: Schaffrath C]]
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[[Category: Spencer, J B.]]
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[[Category: Spencer JB]]
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[[Category: anti-parallel beta sheet]]
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[[Category: central 7 stranded beta sheet]]
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[[Category: fluorinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:31:44 2008''
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Current revision

Crystal structure and mechanism of a bacterial fluorinating enzyme

PDB ID 1rqp

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