2fxl: Difference between revisions

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New page: left|200px<br /><applet load="2fxl" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fxl, resolution 1.76Å" /> '''Urate oxidase from a...
 
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[[Image:2fxl.gif|left|200px]]<br /><applet load="2fxl" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2fxl, resolution 1.76&Aring;" />
'''Urate oxidase from aspergillus flavus complexed with allantoin'''<br />


==Overview==
==Urate oxidase from aspergillus flavus complexed with allantoin==
Urate oxidase from Aspergillus flavus catalyzes the degradation of uric, acid to [S]-allantoin through 5-hydroxyisourate as a metastable, intermediate. The second degradation step is thought either catalyzed by, another specific enzyme, or spontaneous. The structure of the enzyme was, known at high resolution by X-ray diffraction of I222 crystals complexed, with a purine-type inhibitor (8-azaxanthin). Analyzing the X-ray structure, of urate oxidase treated with an excess of urate, the natural substrate, shows unexpectedly that the active site recaptures [S]-allantoin from the, racemic end product of a second degradation step.
<StructureSection load='2fxl' size='340' side='right'caption='[[2fxl]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2fxl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_flavus Aspergillus flavus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FXL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FXL 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]] 1.76&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2AL:1-(2,5-DIOXO-2,5-DIHYDRO-1H-IMIDAZOL-4-YL)UREA'>2AL</scene>, <scene name='pdbligand=SAC:N-ACETYL-SERINE'>SAC</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=2fxl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fxl OCA], [https://pdbe.org/2fxl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fxl RCSB], [https://www.ebi.ac.uk/pdbsum/2fxl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fxl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/URIC_ASPFL URIC_ASPFL] Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin.
== 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/fx/2fxl_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=2fxl ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Urate oxidase from Aspergillus flavus catalyzes the degradation of uric acid to [S]-allantoin through 5-hydroxyisourate as a metastable intermediate. The second degradation step is thought either catalyzed by another specific enzyme, or spontaneous. The structure of the enzyme was known at high resolution by X-ray diffraction of I222 crystals complexed with a purine-type inhibitor (8-azaxanthin). Analyzing the X-ray structure of urate oxidase treated with an excess of urate, the natural substrate, shows unexpectedly that the active site recaptures [S]-allantoin from the racemic end product of a second degradation step.


==About this Structure==
Recapture of [S]-allantoin, the product of the two-step degradation of uric acid, by urate oxidase.,Gabison L, Chiadmi M, Colloc'h N, Castro B, El Hajji M, Prange T FEBS Lett. 2006 Apr 3;580(8):2087-91. Epub 2006 Mar 10. PMID:16545381<ref>PMID:16545381</ref>
2FXL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_flavus Aspergillus flavus] with 2AL as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Urate_oxidase Urate oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.3.3 1.7.3.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FXL OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Recapture of [S]-allantoin, the product of the two-step degradation of uric acid, by urate oxidase., Gabison L, Chiadmi M, Colloc'h N, Castro B, El Hajji M, Prange T, FEBS Lett. 2006 Apr 3;580(8):2087-91. Epub 2006 Mar 10. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16545381 16545381]
</div>
<div class="pdbe-citations 2fxl" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Urate oxidase 3D structures|Urate oxidase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aspergillus flavus]]
[[Category: Aspergillus flavus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Urate oxidase]]
[[Category: Chiadmi M]]
[[Category: Chiadmi, M.]]
[[Category: Colloc'h N]]
[[Category: Gabison, L.]]
[[Category: Gabison L]]
[[Category: H, N.Colloc.]]
[[Category: Prange T]]
[[Category: Prange, T.]]
[[Category: 2AL]]
[[Category: allantoin]]
[[Category: dimeric barrel]]
[[Category: oxidoreductase]]
[[Category: tunnel-shaped protein]]
[[Category: uric acid degradation]]
 
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