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| | <StructureSection load='3cks' size='340' side='right'caption='[[3cks]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='3cks' size='340' side='right'caption='[[3cks]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3cks]] is a 1 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=3CKS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CKS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3cks]] 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=3CKS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CKS FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AZA:8-AZAXANTHINE'>AZA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</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]] 1.7Å</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=AZA:8-AZAXANTHINE'>AZA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</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;'>[[2zka|2zka]], [[2zkb|2zkb]]</div></td></tr>
| + | |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">UAZ, UOX ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5059 ASPFL])</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=3cks FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cks OCA], [https://pdbe.org/3cks PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cks RCSB], [https://www.ebi.ac.uk/pdbsum/3cks PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cks 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=3cks FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cks OCA], [https://pdbe.org/3cks PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cks RCSB], [https://www.ebi.ac.uk/pdbsum/3cks PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cks 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: Abraini, J H]] | + | [[Category: Abraini JH]] |
| - | [[Category: Chiadmi, M]] | + | [[Category: Chiadmi M]] |
| - | [[Category: Gabison, L]] | + | [[Category: Colloc'h N]] |
| - | [[Category: Prange, T]]
| + | [[Category: Gabison L]] |
| - | [[Category: H, N Colloc]]
| + | [[Category: Prange T]] |
| - | [[Category: Acetylation]] | + | |
| - | [[Category: Gaz-protein complex]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Peroxisome]]
| + | |
| - | [[Category: Purine metabolism]]
| + | |
| - | [[Category: T-fold domain]] | + | |
| - | [[Category: Tetramer]]
| + | |
| - | [[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
The localization of dioxygen sites in oxygen-binding proteins is a nontrivial experimental task and is often suggested through indirect methods such as using xenon or halide anions as oxygen probes. In this study, a straightforward method based on x-ray crystallography under high pressure of pure oxygen has been developed. An application is given on urate oxidase (UOX), a cofactorless enzyme that catalyzes the oxidation of uric acid to 5-hydroxyisourate in the presence of dioxygen. UOX crystals in complex with a competitive inhibitor of its natural substrate are submitted to an increasing pressure of 1.0, 2.5, or 4.0 MPa of gaseous oxygen. The results clearly show that dioxygen binds within the active site at a location where a water molecule is usually observed but does not bind in the already characterized specific hydrophobic pocket of xenon. Moreover, crystallizing UOX in the presence of a large excess of chloride (NaCl) shows that one chloride ion goes at the same location as the oxygen. The dioxygen hydrophilic environment (an asparagine, a histidine, and a threonine residues), its absence within the xenon binding site, and its location identical to a water molecule or a chloride ion suggest that the dioxygen site is mainly polar. The implication of the dioxygen location on the mechanism is discussed with respect to the experimentally suggested transient intermediates during the reaction cascade.
Oxygen pressurized X-ray crystallography: probing the dioxygen binding site in cofactorless urate oxidase and implications for its catalytic mechanism.,Colloc'h N, Gabison L, Monard G, Altarsha M, Chiadmi M, Marassio G, Sopkova-de Oliveira Santos J, El Hajji M, Castro B, Abraini JH, Prange T Biophys J. 2008 Sep;95(5):2415-22. Epub 2008 Mar 28. PMID:18375516[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Colloc'h N, Gabison L, Monard G, Altarsha M, Chiadmi M, Marassio G, Sopkova-de Oliveira Santos J, El Hajji M, Castro B, Abraini JH, Prange T. Oxygen pressurized X-ray crystallography: probing the dioxygen binding site in cofactorless urate oxidase and implications for its catalytic mechanism. Biophys J. 2008 Sep;95(5):2415-22. Epub 2008 Mar 28. PMID:18375516 doi:10.1529/biophysj.107.122184
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