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[[Image:2cc2.gif|left|200px]]<br />
<applet load="2cc2" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2cc2, resolution 2.00&Aring;" />
'''X-RAY CRYSTAL STRUCTURE OF 5'-FLUORODEOXYADENOSINE SYNTHASE FROM STREPTOMYCES CATTLEYA COMPLEXED WITH 5'DEOXYADENOSINE'''<br />


==About this Structure==
==X-ray crystal structure of 5'-fluorodeoxyadenosine synthase from Streptomyces cattleya complexed with 5'deoxyadenosine==
2CC2 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 CL and 5AD as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[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]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CC2 OCA]].  
<StructureSection load='2cc2' size='340' side='right'caption='[[2cc2]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
[[Category: Adenosyl-fluoride synthase]]
== Structural highlights ==
[[Category: Single protein]]
<table><tr><td colspan='2'>[[2cc2]] 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=2CC2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CC2 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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5AD:5-DEOXYADENOSINE'>5AD</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=2cc2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cc2 OCA], [https://pdbe.org/2cc2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cc2 RCSB], [https://www.ebi.ac.uk/pdbsum/2cc2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cc2 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/cc/2cc2_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=2cc2 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2cc2" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces cattleya]]
[[Category: Streptomyces cattleya]]
[[Category: Deng, H.]]
[[Category: Deng H]]
[[Category: Hagan, D.O.]]
[[Category: McGlinchey RP]]
[[Category: Mcewan, A.R.]]
[[Category: Mcewan AR]]
[[Category: Mcglinchey, R.P.]]
[[Category: Naismith JH]]
[[Category: Naismith, J.H.]]
[[Category: O'Hagan D]]
[[Category: Robinson, D.R.]]
[[Category: Robinson DR]]
[[Category: Spencer, J.]]
[[Category: Spencer J]]
[[Category: 5AD]]
[[Category: CL]]
[[Category: 5'deoxyadenosine]]
[[Category: fla]]
[[Category: fluorinase]]
[[Category: transferase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:50:21 2007''
Retrieved from "https://proteopedia.org/2cc2"