1r51
From Proteopedia
(New page: 200px<br /><applet load="1r51" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r51, resolution 1.75Å" /> '''URATE OXIDASE FROM A...) |
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| - | [[Image:1r51.gif|left|200px]]<br /><applet load="1r51" size=" | + | [[Image:1r51.gif|left|200px]]<br /><applet load="1r51" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1r51, resolution 1.75Å" /> | caption="1r51, resolution 1.75Å" /> | ||
'''URATE OXIDASE FROM ASPERGILLUS FLAVUS COMPLEXED WITH ITS INHIBITOR 8-AZAXANTHIN'''<br /> | '''URATE OXIDASE FROM ASPERGILLUS FLAVUS COMPLEXED WITH ITS INHIBITOR 8-AZAXANTHIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | High-resolution X-ray structures of the complexes of Aspergillus flavus | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1R51 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_flavus Aspergillus flavus] with AZA and CYS as [http://en.wikipedia.org/wiki/ligands ligands]. This structure | + | 1R51 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_flavus Aspergillus flavus] with <scene name='pdbligand=AZA:'>AZA</scene> and <scene name='pdbligand=CYS:'>CYS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1UOX. Active as [http://en.wikipedia.org/wiki/Urate_oxidase Urate oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.3.3 1.7.3.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R51 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Urate oxidase]] | [[Category: Urate oxidase]] | ||
| - | [[Category: H, N | + | [[Category: H, N Colloc.]] |
[[Category: Prange, T.]] | [[Category: Prange, T.]] | ||
[[Category: Retailleau, P.]] | [[Category: Retailleau, P.]] | ||
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[[Category: uric acid degradation]] | [[Category: uric acid degradation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:47:05 2008'' |
Revision as of 12:47, 21 February 2008
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URATE OXIDASE FROM ASPERGILLUS FLAVUS COMPLEXED WITH ITS INHIBITOR 8-AZAXANTHIN
Overview
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.
About this Structure
1R51 is a Single protein structure of sequence from Aspergillus flavus with and as ligands. This structure supersedes the now removed PDB entry 1UOX. Active as Urate oxidase, with EC number 1.7.3.3 Full crystallographic information is available from OCA.
Reference
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
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