2q37: Difference between revisions
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[[Image:2q37.gif|left|200px]] | [[Image:2q37.gif|left|200px]] | ||
'''Crystal structure of OHCU decarboxylase in the presence of (S)-allantoin''' | {{Structure | ||
|PDB= 2q37 |SIZE=350|CAPTION= <scene name='initialview01'>2q37</scene>, resolution 2.5Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=3AL:1-[(4S)-2,5-DIOXOIMIDAZOLIDIN-4-YL]UREA'>3AL</scene> | |||
|ACTIVITY= | |||
|GENE= TTL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana]) | |||
}} | |||
'''Crystal structure of OHCU decarboxylase in the presence of (S)-allantoin''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2Q37 is a [ | 2Q37 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q37 OCA]. | ||
==Reference== | ==Reference== | ||
Structural and functional basis for (S)-allantoin formation in the ureide pathway., Kim K, Park J, Rhee S, J Biol Chem. 2007 Aug 10;282(32):23457-64. Epub 2007 Jun 13. PMID:[http:// | Structural and functional basis for (S)-allantoin formation in the ureide pathway., Kim K, Park J, Rhee S, J Biol Chem. 2007 Aug 10;282(32):23457-64. Epub 2007 Jun 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17567580 17567580] | ||
[[Category: Arabidopsis thaliana]] | [[Category: Arabidopsis thaliana]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ohcu]] | [[Category: ohcu]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:21:01 2008'' | ||
Revision as of 19:21, 20 March 2008
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| , resolution 2.5Å | |||||||
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| Ligands: | |||||||
| Gene: | TTL (Arabidopsis thaliana) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of OHCU decarboxylase in the presence of (S)-allantoin
OverviewOverview
The ureide pathway, which mediates the oxidative degradation of uric acid to (S)-allantoin, represents the late stage of purine catabolism in most organisms. The details of uric acid metabolism remained elusive until the complete pathway involving three enzymes was recently identified and characterized. However, the molecular details of the exclusive production of one enantiomer of allantoin in this pathway are still undefined. Here we report the crystal structure of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) decarboxylase, which catalyzes the last reaction of the pathway, in a complex with the product, (S)-allantoin, at 2.5-A resolution. The homodimeric helical protein represents a novel structural motif and reveals that the active site in each monomer contains no cofactors, distinguishing this enzyme mechanistically from other cofactor-dependent decarboxylases. On the basis of structural analysis, along with site-directed mutagenesis, a mechanism for the enzyme is proposed in which a decarboxylation reaction occurs directly, and the invariant histidine residue in the OHCU decarboxylase family plays an essential role in producing (S)-allantoin through a proton transfer from the hydroxyl group at C4 to C5 at the re-face of OHCU. These results provide molecular details that address a longstanding question of how living organisms selectively produce (S)-allantoin.
About this StructureAbout this Structure
2Q37 is a Single protein structure of sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.
ReferenceReference
Structural and functional basis for (S)-allantoin formation in the ureide pathway., Kim K, Park J, Rhee S, J Biol Chem. 2007 Aug 10;282(32):23457-64. Epub 2007 Jun 13. PMID:17567580
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