2fxl: Difference between revisions

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[[Image:2fxl.gif|left|200px]]<br /><applet load="2fxl" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2fxl.gif|left|200px]]
caption="2fxl, resolution 1.76&Aring;" />
 
'''Urate oxidase from aspergillus flavus complexed with allantoin'''<br />
{{Structure
|PDB= 2fxl |SIZE=350|CAPTION= <scene name='initialview01'>2fxl</scene>, resolution 1.76&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=2AL:1-(2,5-DIOXO-2,5-DIHYDRO-1H-IMIDAZOL-4-YL)UREA'>2AL</scene>
|ACTIVITY= [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]
|GENE= uaZ, uox ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5059 Aspergillus flavus])
}}
 
'''Urate oxidase from aspergillus flavus complexed with allantoin'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
2FXL 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=2AL:'>2AL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=2FXL OCA].  
2FXL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_flavus Aspergillus flavus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FXL OCA].  


==Reference==
==Reference==
Recapture of [S]-allantoin, the product of the two-step degradation of uric acid, by urate oxidase., Gabison L, Chiadmi M, Colloc'h N, Castro B, El Hajji M, Prange T, FEBS Lett. 2006 Apr 3;580(8):2087-91. Epub 2006 Mar 10. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16545381 16545381]
Recapture of [S]-allantoin, the product of the two-step degradation of uric acid, by urate oxidase., Gabison L, Chiadmi M, Colloc'h N, Castro B, El Hajji M, Prange T, FEBS Lett. 2006 Apr 3;580(8):2087-91. Epub 2006 Mar 10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16545381 16545381]
[[Category: Aspergillus flavus]]
[[Category: Aspergillus flavus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: uric acid degradation]]
[[Category: uric acid degradation]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:26:06 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:57:56 2008''

Revision as of 17:57, 20 March 2008

File:2fxl.gif


PDB ID 2fxl

Drag the structure with the mouse to rotate
, resolution 1.76Å
Ligands:
Gene: uaZ, uox (Aspergillus flavus)
Activity: Urate oxidase, with EC number 1.7.3.3
Coordinates: save as pdb, mmCIF, xml



Urate oxidase from aspergillus flavus complexed with allantoin


OverviewOverview

Urate oxidase from Aspergillus flavus catalyzes the degradation of uric acid to [S]-allantoin through 5-hydroxyisourate as a metastable intermediate. The second degradation step is thought either catalyzed by another specific enzyme, or spontaneous. The structure of the enzyme was known at high resolution by X-ray diffraction of I222 crystals complexed with a purine-type inhibitor (8-azaxanthin). Analyzing the X-ray structure of urate oxidase treated with an excess of urate, the natural substrate, shows unexpectedly that the active site recaptures [S]-allantoin from the racemic end product of a second degradation step.

About this StructureAbout this Structure

2FXL is a Single protein structure of sequence from Aspergillus flavus. Full crystallographic information is available from OCA.

ReferenceReference

Recapture of [S]-allantoin, the product of the two-step degradation of uric acid, by urate oxidase., Gabison L, Chiadmi M, Colloc'h N, Castro B, El Hajji M, Prange T, FEBS Lett. 2006 Apr 3;580(8):2087-91. Epub 2006 Mar 10. PMID:16545381

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