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[[Image:2c2w.gif|left|200px]]<br />
<applet load="2c2w" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2c2w, resolution 2.00&Aring;" />
'''THE FLUORINASE FROM STREPTOMYCES CATTLEYA IS ALSO A CHLORINASE. STRUCTURE OF 5'-CHLORO-5'-DEOXYADENOSINE CRYSTALLISED IN THE FLUORINASE.'''<br />


==About this Structure==
==The fluorinase from Streptomyces cattleya is also a chlorinase. Structure of 5'-chloro-5'-deoxyadenosine crystallised in the fluorinase.==
2C2W 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 5CD 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=2C2W OCA].  
<StructureSection load='2c2w' size='340' side='right'caption='[[2c2w]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 
== Structural highlights ==
==Reference==
<table><tr><td colspan='2'>[[2c2w]] 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=2C2W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C2W FirstGlance]. <br>
The fluorinase from Streptomyces cattleya is also a chlorinase., Deng H, Cobb SL, McEwan AR, McGlinchey RP, Naismith JH, O'Hagan D, Robinson DA, Spencer JB, Angew Chem Int Ed Engl. 2006 Jan 23;45(5):759-62. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16370017 16370017]
</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>
[[Category: Adenosyl-fluoride synthase]]
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5CD:5-CHLORO-5-DEOXYADENOSINE'>5CD</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
[[Category: Single protein]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2c2w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c2w OCA], [https://pdbe.org/2c2w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c2w RCSB], [https://www.ebi.ac.uk/pdbsum/2c2w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c2w 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/c2/2c2w_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=2c2w ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces cattleya]]
[[Category: Streptomyces cattleya]]
[[Category: Hagan, D.O.]]
[[Category: McEwan AR]]
[[Category: Mcewan, A.R.]]
[[Category: Naismith JH]]
[[Category: Naismith, J.H.]]
[[Category: O'Hagan D]]
[[Category: 5CD]]
[[Category: CL]]
[[Category: 5'-chloro-5'-deoxyadenosine]]
[[Category: bacterial chlorinating enzyme]]
[[Category: bacterial fluorinating enzyme]]
[[Category: chlorinase]]
[[Category: fla]]
[[Category: fluorinase]]
[[Category: streptomyces cattleya]]
[[Category: transferase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov  5 17:56:52 2007''

Latest revision as of 17:03, 13 December 2023

The fluorinase from Streptomyces cattleya is also a chlorinase. Structure of 5'-chloro-5'-deoxyadenosine crystallised in the fluorinase.The fluorinase from Streptomyces cattleya is also a chlorinase. Structure of 5'-chloro-5'-deoxyadenosine crystallised in the fluorinase.

Structural highlights

2c2w is a 3 chain structure with sequence from Streptomyces cattleya. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1] [2] [3] [4] [5] [6]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Schaffrath C, Deng H, O'Hagan D. Isolation and characterisation of 5'-fluorodeoxyadenosine synthase, a fluorination enzyme from Streptomyces cattleya. FEBS Lett. 2003 Jul 17;547(1-3):111-4. PMID:12860396
  2. ↑ Dong C, Huang F, Deng H, Schaffrath C, Spencer JB, O'Hagan D, Naismith JH. Crystal structure and mechanism of a bacterial fluorinating enzyme. Nature. 2004 Feb 5;427(6974):561-5. PMID:14765200 doi:http://dx.doi.org/10.1038/nature02280
  3. ↑ Deng H, Cobb SL, McEwan AR, McGlinchey RP, Naismith JH, O'Hagan D, Robinson DA, Spencer JB. The fluorinase from Streptomyces cattleya is also a chlorinase. Angew Chem Int Ed Engl. 2006 Jan 23;45(5):759-62. PMID:16370017 doi:http://dx.doi.org/10.1002/anie.200503582
  4. ↑ Cobb SL, Deng H, McEwan AR, Naismith JH, O'Hagan D, Robinson DA. Substrate specificity in enzymatic fluorination. The fluorinase from Streptomyces cattleya accepts 2'-deoxyadenosine substrates. Org Biomol Chem. 2006 Apr 21;4(8):1458-60. Epub 2006 Mar 8. PMID:16604208 doi:10.1039/b600574h
  5. ↑ Huang F, Haydock SF, Spiteller D, Mironenko T, Li TL, O'Hagan D, Leadlay PF, Spencer JB. The gene cluster for fluorometabolite biosynthesis in Streptomyces cattleya: a thioesterase confers resistance to fluoroacetyl-coenzyme A. Chem Biol. 2006 May;13(5):475-84. PMID:16720268 doi:http://dx.doi.org/S1074-5521(06)00084-6
  6. ↑ Zhu X, Robinson DA, McEwan AR, O'Hagan D, Naismith JH. Mechanism of enzymatic fluorination in Streptomyces cattleya. J Am Chem Soc. 2007 Nov 28;129(47):14597-604. Epub 2007 Nov 7. PMID:17985882 doi:10.1021/ja0731569

2c2w, resolution 2.00Å

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