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==Urate oxidase from aspergillus flavus complexed with allantoin== | |||
<StructureSection load='2fxl' size='340' side='right'caption='[[2fxl]], [[Resolution|resolution]] 1.76Å' 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]] 1.76Å</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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2fxl" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
Urate oxidase | *[[Urate oxidase 3D structures|Urate oxidase 3D structures]] | ||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Aspergillus flavus]] | [[Category: Aspergillus flavus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Chiadmi M]] | ||
[[Category: | [[Category: Colloc'h N]] | ||
[[Category: Gabison | [[Category: Gabison L]] | ||
[[Category: Prange T]] | |||
[[Category: Prange | |||
Latest revision as of 12:33, 30 August 2023
Urate oxidase from aspergillus flavus complexed with allantoinUrate oxidase from aspergillus flavus complexed with allantoin
Structural highlights
FunctionURIC_ASPFL Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin. 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 PubMedUrate 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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