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| | ==Crystal structure of 5-hydroxyisourate Hydrolase (formerly known as TRP, Transthyretin Related Protein)== | | ==Crystal structure of 5-hydroxyisourate Hydrolase (formerly known as TRP, Transthyretin Related Protein)== |
| - | <StructureSection load='2h1x' size='340' side='right' caption='[[2h1x]], [[Resolution|resolution]] 1.98Å' scene=''> | + | <StructureSection load='2h1x' size='340' side='right'caption='[[2h1x]], [[Resolution|resolution]] 1.98Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2h1x]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Brachidanio_rerio Brachidanio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H1X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2H1X FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2h1x]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H1X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H1X FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1f41|1f41]]</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]] 1.98Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GeneID:558664 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7955 Brachidanio rerio])</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=2h1x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h1x OCA], [https://pdbe.org/2h1x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h1x RCSB], [https://www.ebi.ac.uk/pdbsum/2h1x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h1x 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/Hydroxyisourate_hydrolase Hydroxyisourate hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.17 3.5.2.17] </span></td></tr>
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| - | <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=2h1x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h1x OCA], [http://pdbe.org/2h1x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2h1x RCSB], [http://www.ebi.ac.uk/pdbsum/2h1x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2h1x ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HIUH_DANRE HIUH_DANRE]] Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU). | + | [https://www.uniprot.org/uniprot/HIUH_DANRE HIUH_DANRE] Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU). |
| | == 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== |
| - | *[[Transthyretin|Transthyretin]] | + | *[[Transthyretin 3D structures|Transthyretin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Brachidanio rerio]] | + | [[Category: Danio rerio]] |
| - | [[Category: Hydroxyisourate hydrolase]] | + | [[Category: Large Structures]] |
| - | [[Category: Berni, R]] | + | [[Category: Berni R]] |
| - | [[Category: Cendron, L]] | + | [[Category: Cendron L]] |
| - | [[Category: Folli, C]] | + | [[Category: Folli C]] |
| - | [[Category: Percudani, R]] | + | [[Category: Percudani R]] |
| - | [[Category: Ramazzina, I]] | + | [[Category: Ramazzina I]] |
| - | [[Category: Zanotti, G]] | + | [[Category: Zanotti G]] |
| - | [[Category: 5-hydroxyisourate hydrolase]]
| + | |
| - | [[Category: Allantoin]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Trp]]
| + | |
| - | [[Category: Uric acid degradation]]
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| Structural highlights
Function
HIUH_DANRE Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU).
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
During early vertebrate evolution, a duplication event in the gene encoding 5-hydroxyisourate hydrolase (HIUase), a widely distributed enzyme of purine metabolism, gave rise to transthyretin (TTR), a thyroid hormone transporter. We report here on the crystal structure of zebra fish HIUase in two different crystal forms. Despite the phylogenetic distance, this structure compares well with those of newly characterized bacterial HIUases, especially with regard to catalytic regions, which are highly preserved. Comparison with TTR structure reveals a highly conserved scaffold, harbouring distinct functional sites located in the same regions of the two vertebrate proteins. Residues that are differentially conserved in HIUases compared to TTR map in putative catalytic regions occupying significant portions of the two halves of a central channel that transverses the whole TTR protein. The evolution of TTR has been accompanied by remarkable changes of the HIUase active sites that gave rise to a channel open at both ends, thus allowing free access to hormone molecules.
Structure of zebra fish HIUase: insights into evolution of an enzyme to a hormone transporter.,Zanotti G, Cendron L, Ramazzina I, Folli C, Percudani R, Berni R J Mol Biol. 2006 Oct 13;363(1):1-9. Epub 2006 Aug 2. PMID:16952372[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zanotti G, Cendron L, Ramazzina I, Folli C, Percudani R, Berni R. Structure of zebra fish HIUase: insights into evolution of an enzyme to a hormone transporter. J Mol Biol. 2006 Oct 13;363(1):1-9. Epub 2006 Aug 2. PMID:16952372 doi:10.1016/j.jmb.2006.07.079
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