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| | <StructureSection load='1xxj' size='340' side='right'caption='[[1xxj]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='1xxj' size='340' side='right'caption='[[1xxj]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1xxj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspfl Aspfl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XXJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XXJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1xxj]] is a 4 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=1XXJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XXJ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BNZ:BENZENE'>BNZ</scene>, <scene name='pdbligand=UNC:5-AMINO-6-NITROPYRIMIDINE-2,4(1H,3H)-DIONE'>UNC</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]] 2.8Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAC:N-ACETYL-SERINE'>SAC</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BNZ:BENZENE'>BNZ</scene>, <scene name='pdbligand=SAC:N-ACETYL-SERINE'>SAC</scene>, <scene name='pdbligand=UNC:5-AMINO-6-NITROPYRIMIDINE-2,4(1H,3H)-DIONE'>UNC</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1wrr|1wrr]]</div></td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Factor_independent_urate_hydroxylase Factor independent urate hydroxylase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=1xxj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xxj OCA], [https://pdbe.org/1xxj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xxj RCSB], [https://www.ebi.ac.uk/pdbsum/1xxj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xxj ProSAT]</span></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=1xxj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xxj OCA], [https://pdbe.org/1xxj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xxj RCSB], [https://www.ebi.ac.uk/pdbsum/1xxj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xxj ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == 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.
| + | [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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| | ==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: Aspfl]] | + | [[Category: Aspergillus flavus]] |
| - | [[Category: Factor independent urate hydroxylase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bonnete, F]] | + | [[Category: Bonnete F]] |
| - | [[Category: Castro, B]] | + | [[Category: Castro B]] |
| - | [[Category: Hajji, M El]] | + | [[Category: Colloc'h N]] |
| - | [[Category: Prange, T]] | + | [[Category: El Hajji M]] |
| - | [[Category: Retailleau, P]] | + | [[Category: Prange T]] |
| - | [[Category: Vivares, D]] | + | [[Category: Retailleau P]] |
| - | [[Category: H, N Colloc]]
| + | [[Category: Vivares D]] |
| - | [[Category: Dimeric barrel]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Tunnel-shaped protein]]
| + | |
| - | [[Category: Uric acid degradation]]
| + | |
| 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 from Aspergillus flavus (uricase or Uox; EC 1.7.3.3) is a 135 kDa homotetramer with a subunit consisting of 301 amino acids. It catalyses the first step of the degradation of uric acid into allantoin. The structure of the extracted enzyme complexed with a purine-type inhibitor (8-azaxanthin) had been solved from high-resolution X-ray diffraction of I222 crystals. Expression of the recombinant enzyme in Saccharomyces cerevisiae followed by a new purification procedure allowed the crystallization of both unliganded and liganded enzymes utilizing the same conditions but in various crystal forms. Here, four different crystal forms of Uox are analyzed. The diversity of the Uox crystal forms appears to depend strongly on the chemicals used as inhibitors. In the presence of uracil and 5,6-diaminouracil crystals usually belong to the trigonal space group P3(1)21, the asymmetric unit (AU) of which contains one tetramer of Uox (four subunits). Chemical oxidation of 5,6-diaminouracil within the protein may occur, leading to the canonical (I222) packing with one subunit per AU. Coexistence of two crystal forms, P2(1) with two tetramers per AU and I222, was found in the same crystallization drop containing another inhibitor, guanine. Finally, a fourth form, P2(1)2(1)2 with one tetramer per AU, resulted fortuitously in the presence of cymelarsan, an additive. Of all the reported forms, the I222 crystal forms present by far the best X-ray diffraction resolution (approximately 1.6 angstroms resolution compared with 2.3-3.2 angstroms for the other forms). The various structures and contacts in all crystalline lattices are compared. The backbones are essentially conserved except for the region near the active site. Its location at the dimer interface is thus likely to be at the origin of the crystal contact changes as a response to the various bound inhibitors.
Urate oxidase from Aspergillus flavus: new crystal-packing contacts in relation to the content of the active site.,Retailleau P, Colloc'h N, Vivares D, Bonnete F, Castro B, El Hajji M, Prange T Acta Crystallogr D Biol Crystallogr. 2005 Mar;61(Pt 3):218-29. Epub 2005, Feb 24. PMID:15735331[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Retailleau P, Colloc'h N, Vivares D, Bonnete F, Castro B, El Hajji M, Prange T. Urate oxidase from Aspergillus flavus: new crystal-packing contacts in relation to the content of the active site. Acta Crystallogr D Biol Crystallogr. 2005 Mar;61(Pt 3):218-29. Epub 2005, Feb 24. PMID:15735331 doi:http://dx.doi.org/10.1107/S0907444904031531
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