2c4u: Difference between revisions

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OCA

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-[[Image:2c4u.gif|left|200px]]<br />
-<applet load="2c4u" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="2c4u, resolution 2.50&Aring;" />
-'''CRYSTAL STRUCTURE OF THE APO FORM OF THE 5'-FLUORO-5'-DEOXYADENOSINE SYNTHASE ENZYME FROM STREPTOMYCES CATTLEYA'''<br />
-==Overview==
+==Crystal structure of the apo form of the 5'-Fluoro-5'-deoxyadenosine synthase enzyme from Streptomyces cattleya==
-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.
+<StructureSection load='2c4u' size='340' side='right'caption='[[2c4u]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2c4u]] is a 6 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=2C4U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C4U 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]] 2.5&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=2c4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c4u OCA], [https://pdbe.org/2c4u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c4u RCSB], [https://www.ebi.ac.uk/pdbsum/2c4u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c4u 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/c4/2c4u_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=2c4u 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.
-==About this Structure==
+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>
-C4U is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Streptomyces_cattleya Streptomyces cattleya]] with GOL as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.63 2.5.1.63]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C4U OCA]].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16604208 16604208]
+</div>
-[[Category: Single protein]]
+<div class="pdbe-citations 2c4u" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Streptomyces cattleya]]
-[[Category: Delaurentis, W.]]
+[[Category: DeLaurentis W]]
-[[Category: Deng, H.]]
+[[Category: Deng H]]
-[[Category: Hagan, D.O.]]
+[[Category: McEwan AR]]
-[[Category: Mcewan, A.R.]]
+[[Category: McGlinchey RP]]
-[[Category: Mcglinchey, R.P.]]
+[[Category: Naismith JH]]
-[[Category: Naismith, J.H.]]
+[[Category: O'Hagan D]]
-[[Category: Robinson, D.A.]]
+[[Category: Robinson DA]]
-[[Category: GOL]]
-[[Category: 5'-fluorodeoxyadanosine synthase]]
-[[Category: apo]]
-[[Category: fda]]
-[[Category: fluorinase]]
-[[Category: sam]]
-[[Category: transferase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 18:59:45 2007''