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| | ==URATE OXIDASE AZIDE URIC ACID TERNARY complex== | | ==URATE OXIDASE AZIDE URIC ACID TERNARY complex== |
| - | <StructureSection load='4pr8' size='340' side='right' caption='[[4pr8]], [[Resolution|resolution]] 1.16Å' scene=''> | + | <StructureSection load='4pr8' size='340' side='right'caption='[[4pr8]], [[Resolution|resolution]] 1.16Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4pr8]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PR8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PR8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4pr8]] 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=4PR8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PR8 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AZI:AZIDE+ION'>AZI</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=URC:URIC+ACID'>URC</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.16Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=AZI:AZIDE+ION'>AZI</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=URC:URIC+ACID'>URC</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3p9f|3p9f]], [[4fsk|4fsk]], [[4oqc|4oqc]], [[4poe|4poe]], [[3bjp|3bjp]], [[3ld4|3ld4]], [[4puv|4puv]]</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=4pr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pr8 OCA], [https://pdbe.org/4pr8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pr8 RCSB], [https://www.ebi.ac.uk/pdbsum/4pr8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pr8 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Factor_independent_urate_hydroxylase Factor independent urate hydroxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.3.3 1.7.3.3] </span></td></tr>
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pr8 OCA], [http://pdbe.org/4pr8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pr8 RCSB], [http://www.ebi.ac.uk/pdbsum/4pr8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pr8 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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. | + | [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. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Urate Oxidase|Urate Oxidase]] | + | *[[Urate oxidase 3D structures|Urate oxidase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Factor independent urate hydroxylase]] | + | [[Category: Aspergillus flavus]] |
| - | [[Category: Prange, T]] | + | [[Category: Large Structures]] |
| - | [[Category: H, N Colloc]] | + | [[Category: Colloc'h N]] |
| - | [[Category: Degradation mechanism]] | + | [[Category: Prange T]] |
| - | [[Category: Heterotetramer]]
| + | |
| - | [[Category: Inhibition]]
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| - | [[Category: Oxidoreductase]]
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| - | [[Category: Oxygen binding]]
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| - | [[Category: Peroxisome]]
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| - | [[Category: Purine metabolism]]
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| Structural highlights
Function
URIC_ASPFL Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin.
Publication Abstract from PubMed
The inhibition of urate oxidase (UOX) by azide was investigated by X-ray diffraction techniques and compared with cyanide inhibition. Two well characterized sites for reagents are present in the enzyme: the dioxygen site and the substrate-binding site. To examine the selectivity of these sites towards azide inhibition, several crystallization conditions were developed. UOX was co-crystallized with azide (N3) in the presence or absence of either uric acid (UA, the natural substrate) or 8-azaxanthine (8AZA, a competitive inhibitor). In a second set of experiments, previously grown orthorhombic crystals of the UOX-UA or UOX-8AZA complexes were soaked in sodium azide solutions. In a third set of experiments, orthorhombic crystals of UOX with the exchangeable ligand 8-nitroxanthine (8NXN) were soaked in a solution containing uric acid and azide simultaneously (competitive soaking). In all assays, the soaking periods were either short (a few hours) or long (one or two months). These different experimental conditions showed that one or other of the sites, or the two sites together, could be inhibited. This also demonstrated that azide not only competes with dioxygen as cyanide does but also competes with the substrate for its enzymatic site. A model in agreement with experimental data would be an azide in equilibrium between two sites, kinetically in favour of the dioxygen site and thermodynamically in favour of the substrate-binding site.
Azide inhibition of urate oxidase.,Gabison L, Colloc'h N, Prange T Acta Crystallogr F Struct Biol Commun. 2014 Jul;70(Pt 7):896-902. doi:, 10.1107/S2053230X14011753. Epub 2014 Jun 18. PMID:25005084[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gabison L, Colloc'h N, Prange T. Azide inhibition of urate oxidase. Acta Crystallogr F Struct Biol Commun. 2014 Jul;70(Pt 7):896-902. doi:, 10.1107/S2053230X14011753. Epub 2014 Jun 18. PMID:25005084 doi:http://dx.doi.org/10.1107/S2053230X14011753
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