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| | ==Urate oxidase complexed with 8-nitro xanthine== | | ==Urate oxidase complexed with 8-nitro xanthine== |
| - | <StructureSection load='3ld4' size='340' side='right' caption='[[3ld4]], [[Resolution|resolution]] 1.35Å' scene=''> | + | <StructureSection load='3ld4' size='340' side='right'caption='[[3ld4]], [[Resolution|resolution]] 1.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ld4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspfl Aspfl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LD4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LD4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ld4]] 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=3LD4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LD4 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=8NX:8-NITRO-3,7-DIHYDRO-1H-PURINE-2,6-DIONE'>8NX</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 1.35Å</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=8NX:8-NITRO-3,7-DIHYDRO-1H-PURINE-2,6-DIONE'>8NX</scene>, <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1r51|1r51]], [[3l8w|3l8w]], [[3l9g|3l9g]], [[3lbg|3lbg]]</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=3ld4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ld4 OCA], [https://pdbe.org/3ld4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ld4 RCSB], [https://www.ebi.ac.uk/pdbsum/3ld4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ld4 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>
| + | |
| - | <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=3ld4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ld4 OCA], [http://pdbe.org/3ld4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ld4 RCSB], [http://www.ebi.ac.uk/pdbsum/3ld4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ld4 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. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </div> | | </div> |
| | <div class="pdbe-citations 3ld4" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 3ld4" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Urate oxidase 3D structures|Urate oxidase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aspfl]] | |
| - | [[Category: Factor independent urate hydroxylase]] | |
| - | [[Category: Gabison, L]] | |
| - | [[Category: Prange, T]] | |
| - | [[Category: H, N Colloc]] | |
| | [[Category: Aspergillus flavus]] | | [[Category: Aspergillus flavus]] |
| - | [[Category: Nitroxanthine]] | + | [[Category: Large Structures]] |
| - | [[Category: Oxidoreductase]] | + | [[Category: Colloc'h N]] |
| - | [[Category: Peroxisome]] | + | [[Category: Gabison L]] |
| - | [[Category: Protonation]] | + | [[Category: Prange T]] |
| - | [[Category: Purine metabolism]]
| + | |
| - | [[Category: Thioxanthine]]
| + | |
| - | [[Category: Urate oxidase]]
| + | |
| - | [[Category: Xanthine]]
| + | |
| Structural highlights
Function
URIC_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 PubMed
Urate oxidase (uricase; EC 1.7.3.3; UOX) from Aspergillus flavus catalyzes the oxidation of uric acid in the presence of molecular oxygen to 5-hydroxyisourate in the degradation cascade of purines; intriguingly, catalysis proceeds using neither a metal ion (Fe, Cu etc.) nor a redox cofactor. UOX is a tetrameric enzyme with four active sites located at the interface of two subunits; its structure was refined at atomic resolution (1 A) using new crystal data in the presence of xanthine and at near-atomic resolution (1.3-1.7 A) in complexes with the natural substrate (urate) and two inhibitors: 8-nitroxanthine and 8-thiouric acid. Three new features of the structural and mechanistic behaviour of the enzyme were addressed. Firstly, the high resolution of the UOX-xanthine structure allowed the solution of an old structural problem at a contact zone within the tetramer; secondly, the protonation state of the substrate was determined from both a halochromic inhibitor complex (UOX-8-nitroxanthine) and from the H-atom distribution in the active site, using the structures of the UOX-xanthine and the UOX-uric acid complexes; and thirdly, it was possible to extend the general base system, characterized by the conserved catalytic triad Thr-Lys-His, to a large water network that is able to buffer and shuttle protons back and forth between the substrate and the peroxo hole along the reaction pathway.
Near-atomic resolution structures of urate oxidase complexed with its substrate and analogues: the protonation state of the ligand.,Gabison L, Chiadmi M, El Hajji M, Castro B, Colloc'h N, Prange T Acta Crystallogr D Biol Crystallogr. 2010 Jun;66(Pt 6):714-24. Epub 2010 May 15. PMID:20516624[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gabison L, Chiadmi M, El Hajji M, Castro B, Colloc'h N, Prange T. Near-atomic resolution structures of urate oxidase complexed with its substrate and analogues: the protonation state of the ligand. Acta Crystallogr D Biol Crystallogr. 2010 Jun;66(Pt 6):714-24. Epub 2010 May 15. PMID:20516624 doi:10.1107/S090744491001142X
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