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| | ==Crystal structure of Puue Allantoinase complexed with ACA== | | ==Crystal structure of Puue Allantoinase complexed with ACA== |
| - | <StructureSection load='3cl8' size='340' side='right' caption='[[3cl8]], [[Resolution|resolution]] 2.25Å' scene=''> | + | <StructureSection load='3cl8' size='340' side='right'caption='[[3cl8]], [[Resolution|resolution]] 2.25Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3cl8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_fluorescens_liquefaciens"_flugge_1886 "bacillus fluorescens liquefaciens" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CL8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CL8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3cl8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CL8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CL8 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5AC:5-AMINO-1H-IMIDAZOLE-4-CARBOXAMIDE'>5AC</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]] 2.25Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1z7a|1z7a]], [[3cl6|3cl6]], [[3cl7|3cl7]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5AC:5-AMINO-1H-IMIDAZOLE-4-CARBOXAMIDE'>5AC</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Allantoinase Allantoinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.5 3.5.2.5] </span></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=3cl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cl8 OCA], [https://pdbe.org/3cl8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cl8 RCSB], [https://www.ebi.ac.uk/pdbsum/3cl8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cl8 ProSAT]</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=3cl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cl8 OCA], [http://pdbe.org/3cl8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3cl8 RCSB], [http://www.ebi.ac.uk/pdbsum/3cl8 PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q3KFK7_PSEPF Q3KFK7_PSEPF] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cl/3cl8_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cl/3cl8_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus fluorescens liquefaciens flugge 1886]] | + | [[Category: Large Structures]] |
| - | [[Category: Allantoinase]] | + | [[Category: Pseudomonas fluorescens]] |
| - | [[Category: Berni, R]] | + | [[Category: Berni R]] |
| - | [[Category: Cendron, L]] | + | [[Category: Cendron L]] |
| - | [[Category: Folli, C]] | + | [[Category: Folli C]] |
| - | [[Category: Monteverdi, D]] | + | [[Category: Monteverdi D]] |
| - | [[Category: Percudani, R]] | + | [[Category: Percudani R]] |
| - | [[Category: Ramazzina, I]] | + | [[Category: Ramazzina I]] |
| - | [[Category: Zanotti, G]] | + | [[Category: Zanotti G]] |
| - | [[Category: Allantoine]]
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| - | [[Category: Amino imidazole carboximide]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Uric acid degradation]]
| + | |
| Structural highlights
Function
Q3KFK7_PSEPF
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
The hydrolytic cleavage of the hydantoin ring of allantoin, catalyzed by allantoinase, is required for the utilization of the nitrogen present in purine-derived compounds. The allantoinase gene (DAL1), however, is missing in many completely sequenced organisms able to use allantoin as a nitrogen source. Here we show that an alternative allantoinase gene (puuE) can be precisely identified by analyzing its logic relationship with three other genes of the pathway. The novel allantoinase is annotated in structure and sequence data bases as polysaccharide deacetylase for its homology with enzymes that catalyze hydrolytic reactions on chitin or peptidoglycan substrates. The recombinant PuuE protein from Pseudomonas fluorescens exhibits metal-independent allantoinase activity and stereospecificity for the S enantiomer of allantoin. The crystal structures of the protein and of protein-inhibitor complexes reveal an overall similarity with the polysaccharide deacetylase beta/alpha barrel and remarkable differences in oligomeric assembly and active site geometry. The conserved Asp-His-His metal-binding triad is replaced by Glu-His-Trp, a configuration that is distinctive of PuuE proteins within the protein family. An extra domain at the top of the barrel offers a scaffold for protein tetramerization and forms a small substrate-binding cleft by hiding the large binding groove of polysaccharide deacetylases. Substrate positioning at the active site suggests an acid/base mechanism of catalysis in which only one member of the catalytic pair of polysaccharide deacetylases has been conserved. These data provide a structural rationale for the shifting of substrate specificity that occurred during evolution.
Logical identification of an allantoinase analog (puuE) recruited from polysaccharide deacetylases.,Ramazzina I, Cendron L, Folli C, Berni R, Monteverdi D, Zanotti G, Percudani R J Biol Chem. 2008 Aug 22;283(34):23295-304. Epub 2008 Jun 12. PMID:18550550[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ramazzina I, Cendron L, Folli C, Berni R, Monteverdi D, Zanotti G, Percudani R. Logical identification of an allantoinase analog (puuE) recruited from polysaccharide deacetylases. J Biol Chem. 2008 Aug 22;283(34):23295-304. Epub 2008 Jun 12. PMID:18550550 doi:10.1074/jbc.M801195200
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