2cbx: Difference between revisions

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[[Image:2cbx.png|left|200px]]


{{STRUCTURE_2cbx| PDB=2cbx | SCENE= }}
==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]] 2.00&Aring;' 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]] 2&#8491;</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.


===X-RAY CRYSTAL STRUCTURE OF 5'-FLUORODEOXYADENOSINE SYNTHASE FROM STREPTOMYCES CATTLEYA COMPLEXED WITH BETA-D-ERYTHROFURANOSYL-ADENOSINE===
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>


{{ABSTRACT_PUBMED_16604208}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
==About this Structure==
<div class="pdbe-citations 2cbx" style="background-color:#fffaf0;"></div>
[[2cbx]] is a 3 chain structure with 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=2CBX OCA].
== References ==
 
<references/>
==Reference==
__TOC__
<ref group="xtra">PMID:016604208</ref><references group="xtra"/>
</StructureSection>
[[Category: Adenosyl-fluoride synthase]]
[[Category: Large Structures]]
[[Category: Streptomyces cattleya]]
[[Category: Cadicamo, C D.]]
[[Category: Deng, H.]]
[[Category: Hagan, D O.]]
[[Category: Mcewan, A R.]]
[[Category: Mcglinchey, R P.]]
[[Category: Naismith, J H.]]
[[Category: Robinson, D R.]]
[[Category: Spencer, J.]]
[[Category: 5'-fluorodeoxyadenosine synthase]]
[[Category: Aza]]
[[Category: Fla]]
[[Category: Fluorinase]]
[[Category: Inhibitor]]
[[Category: Sam analogue]]
[[Category: Streptomyces cattleya]]
[[Category: Streptomyces cattleya]]
[[Category: Transferase]]
[[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]]

Latest revision as of 17:12, 13 December 2023

X-ray crystal structure of 5'-fluorodeoxyadenosine synthase from Streptomyces cattleya complexed with beta-D-erythrofuranosyl- adenosineX-ray crystal structure of 5'-fluorodeoxyadenosine synthase from Streptomyces cattleya complexed with beta-D-erythrofuranosyl- adenosine

Structural highlights

2cbx 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.

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[7]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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
  7. ↑ 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

2cbx, resolution 2.00Å

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