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2cbx
From Proteopedia
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| - | [[Image:2cbx.gif|left|200px]]<br /> | ||
| - | <applet load="2cbx" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2cbx, resolution 2.00Å" /> | ||
| - | '''X-RAY CRYSTAL STRUCTURE OF 5'-FLUORODEOXYADENOSINE SYNTHASE FROM STREPTOMYCES CATTLEYA COMPLEXED WITH BETA-D-ERYTHROFURANOSYL-ADENOSINE'''<br /> | ||
| - | == | + | ==X-ray crystal structure of 5'-fluorodeoxyadenosine synthase from Streptomyces cattleya complexed with beta-D-erythrofuranosyl- adenosine== |
| - | + | <StructureSection load='2cbx' size='340' side='right'caption='[[2cbx]], [[Resolution|resolution]] 2.00Å' scene=''> | |
| - | [ | + | == Structural highlights == |
| - | [[ | + | <table><tr><td colspan='2'>[[2cbx]] 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=2CBX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CBX FirstGlance]. <br> |
| - | [[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | [[ | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CC5:BETA-D-ERYTHROFURANOSYL-ADENOSINE'>CC5</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2cbx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cbx OCA], [https://pdbe.org/2cbx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cbx RCSB], [https://www.ebi.ac.uk/pdbsum/2cbx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cbx ProSAT]</span></td></tr> | |
| - | [ | + | </table> |
| - | [ | + | == Function == |
| - | [ | + | [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> |
| - | [ | + | == Evolutionary Conservation == |
| - | [ | + | [[Image:Consurf_key_small.gif|200px|right]] |
| - | + | Check<jmol> | |
| - | + | <jmolCheckbox> | |
| - | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cb/2cbx_consurf.spt"</scriptWhenChecked> | |
| - | [ | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| - | + | <text>to colour the structure by Evolutionary Conservation</text> | |
| - | [[ | + | </jmolCheckbox> |
| - | [ | + | </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=2cbx ConSurf]. |
| - | [[ | + | <div style="clear:both"></div> |
| - | [ | + | <div style="background-color:#fffaf0;"> |
| - | + | == Publication Abstract from PubMed == | |
| - | + | The fluorinase enzyme from Streptomyces cattleya displays an unusual ability in biocatalysis in that it forms a C-F bond. We now report that the enzyme will accept 2'-deoxyadenosine in place of adenosine substrates, and structural evidence reveals a reorganisation in hydrogen bonding to accommodate this substrate series. It emerges from this study that the enzyme does not require a planar ribose conformation of the substrate to catalyse C-F bond formation. | |
| - | '' | + | Substrate specificity in enzymatic fluorination. The fluorinase from Streptomyces cattleya accepts 2'-deoxyadenosine substrates.,Cobb SL, Deng H, McEwan AR, Naismith JH, O'Hagan D, Robinson DA Org Biomol Chem. 2006 Apr 21;4(8):1458-60. Epub 2006 Mar 8. PMID:16604208<ref>PMID:16604208</ref> |
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2cbx" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Streptomyces cattleya]] | ||
| + | [[Category: Cadicamo CD]] | ||
| + | [[Category: Deng H]] | ||
| + | [[Category: McEwan AR]] | ||
| + | [[Category: McGlinchey RP]] | ||
| + | [[Category: Naismith JH]] | ||
| + | [[Category: O'Hagan D]] | ||
| + | [[Category: Robinson DR]] | ||
| + | [[Category: Spencer J]] | ||
Current revision
X-ray crystal structure of 5'-fluorodeoxyadenosine synthase from Streptomyces cattleya complexed with beta-D-erythrofuranosyl- adenosine
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