|
|
(One intermediate revision not shown.) |
Line 3: |
Line 3: |
| <StructureSection load='1r4u' size='340' side='right'caption='[[1r4u]], [[Resolution|resolution]] 1.65Å' scene=''> | | <StructureSection load='1r4u' size='340' side='right'caption='[[1r4u]], [[Resolution|resolution]] 1.65Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[1r4u]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspergillus_flavus Aspergillus flavus]. The September 2009 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Xanthine Oxidoreductase'' by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2009_9 10.2210/rcsb_pdb/mom_2009_9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R4U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1R4U FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1r4u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_flavus Aspergillus flavus]. The September 2009 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Xanthine Oxidoreductase'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2009_9 10.2210/rcsb_pdb/mom_2009_9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R4U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R4U FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=OXC:OXONIC+ACID'>OXC</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]] 1.65Å</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=OXC:OXONIC+ACID'>OXC</scene>, <scene name='pdbligand=SAC:N-ACETYL-SERINE'>SAC</scene></td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1r4s|1r4s]], [[1r51|1r51]], [[1r56|1r56]]</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=1r4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r4u OCA], [https://pdbe.org/1r4u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r4u RCSB], [https://www.ebi.ac.uk/pdbsum/1r4u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r4u 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=1r4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r4u OCA], [http://pdbe.org/1r4u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1r4u RCSB], [http://www.ebi.ac.uk/pdbsum/1r4u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1r4u 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]] |
Line 33: |
Line 31: |
| | | |
| ==See Also== | | ==See Also== |
- | *[[Urate Oxidase|Urate Oxidase]] | + | *[[Urate oxidase 3D structures|Urate oxidase 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
Line 39: |
Line 37: |
| </StructureSection> | | </StructureSection> |
| [[Category: Aspergillus flavus]] | | [[Category: Aspergillus flavus]] |
- | [[Category: Factor independent urate hydroxylase]] | |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: RCSB PDB Molecule of the Month]] | | [[Category: RCSB PDB Molecule of the Month]] |
| [[Category: Xanthine Oxidoreductase]] | | [[Category: Xanthine Oxidoreductase]] |
- | [[Category: Prange, T]] | + | [[Category: Colloc'h N]] |
- | [[Category: Retailleau, P]]
| + | [[Category: Prange T]] |
- | [[Category: H, N Colloc]]
| + | [[Category: Retailleau P]] |
- | [[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
High-resolution X-ray structures of the complexes of Aspergillus flavus urate oxidase (Uox) with three inhibitors, 8-azaxanthin (AZA), 9-methyl uric acid (MUA) and oxonic acid (OXC), were determined in an orthorhombic space group (I222). In addition, the ligand-free enzyme was also crystallized in a monoclinic form (P2(1)) and its structure determined. Higher accuracy in the three new enzyme-inhibitor complex structures (Uox-AZA, Uox-MUA and Uox-OXC) with respect to the previously determined structure of Uox-AZA (PDB code 1uox) leads to a reversed position of the inhibitor in the active site of the enzyme. The corrected anchoring of the substrate (uric acid) allows an improvement in the understanding of the enzymatic mechanism of urate oxidase.
Complexed and ligand-free high-resolution structures of urate oxidase (Uox) from Aspergillus flavus: a reassignment of the active-site binding mode.,Retailleau P, Colloc'h N, Vivares D, Bonnete F, Castro B, El-Hajji M, Mornon JP, Monard G, Prange T Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):453-62. Epub 2004, Feb 25. PMID:14993669[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, Mornon JP, Monard G, Prange T. Complexed and ligand-free high-resolution structures of urate oxidase (Uox) from Aspergillus flavus: a reassignment of the active-site binding mode. Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):453-62. Epub 2004, Feb 25. PMID:14993669 doi:http://dx.doi.org/10.1107/S0907444903029718
|