1rqr

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{{Seed}}
 
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[[Image:1rqr.png|left|200px]]
 
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==Crystal structure and mechanism of a bacterial fluorinating enzyme, product complex==
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The line below this paragraph, containing "STRUCTURE_1rqr", creates the "Structure Box" on the page.
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<StructureSection load='1rqr' size='340' side='right'caption='[[1rqr]], [[Resolution|resolution]] 2.67&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1rqr]] 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=1RQR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RQR FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.67&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5FD:5-FLUORO-5-DEOXYADENOSINE'>5FD</scene>, <scene name='pdbligand=MET:METHIONINE'>MET</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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{{STRUCTURE_1rqr| PDB=1rqr | SCENE= }}
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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=1rqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rqr OCA], [https://pdbe.org/1rqr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rqr RCSB], [https://www.ebi.ac.uk/pdbsum/1rqr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rqr ProSAT]</span></td></tr>
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</table>
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== Function ==
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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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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rq/1rqr_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1rqr ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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===Crystal structure and mechanism of a bacterial fluorinating enzyme, product complex===
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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:14765200<ref>PMID:14765200</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_14765200}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1rqr" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 14765200 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_14765200}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1RQR 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=1RQR OCA].
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==Reference==
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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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[[Category: Adenosyl-fluoride synthase]]
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[[Category: Single protein]]
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[[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 Mon Jul 28 17:28:52 2008''
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Current revision

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

PDB ID 1rqr

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