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| | <StructureSection load='5e5c' size='340' side='right'caption='[[5e5c]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='5e5c' size='340' side='right'caption='[[5e5c]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5e5c]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseae Pseae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E5C OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5E5C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5e5c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E5C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5E5C FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.1Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dht, PA0441 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208964 PSEAE])</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=5e5c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e5c OCA], [https://pdbe.org/5e5c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e5c RCSB], [https://www.ebi.ac.uk/pdbsum/5e5c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e5c 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/Dihydropyrimidinase Dihydropyrimidinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.2 3.5.2.2] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5e5c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e5c OCA], [http://pdbe.org/5e5c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e5c RCSB], [http://www.ebi.ac.uk/pdbsum/5e5c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e5c ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HYDA_PSEAE HYDA_PSEAE]] Catalyzes the hydrolysis of dihydropyrimidines and of the structurally related DL-5-mono-substituted hydantoins, to produce N-carbamoyl-D-amino acids. | + | [https://www.uniprot.org/uniprot/HYDA_PSEAE HYDA_PSEAE] Catalyzes the hydrolysis of dihydropyrimidines and of the structurally related DL-5-mono-substituted hydantoins, to produce N-carbamoyl-D-amino acids. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Dihydropyrimidinase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pseae]] | + | [[Category: Pseudomonas aeruginosa PAO1]] |
| - | [[Category: Chen, C J]] | + | [[Category: Chen CJ]] |
| - | [[Category: Hsieh, Y C]] | + | [[Category: Hsieh YC]] |
| - | [[Category: Huang, C C]] | + | [[Category: Huang CC]] |
| - | [[Category: Huang, C Y]] | + | [[Category: Huang CY]] |
| - | [[Category: Huang, Y H]] | + | [[Category: Huang YH]] |
| - | [[Category: Tzeng, C T]] | + | [[Category: Tzeng CT]] |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
HYDA_PSEAE Catalyzes the hydrolysis of dihydropyrimidines and of the structurally related DL-5-mono-substituted hydantoins, to produce N-carbamoyl-D-amino acids.
Publication Abstract from PubMed
Dihydropyrimidinase, a tetrameric metalloenzyme, is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase, hydantoinase, and imidase. In this paper, we report the crystal structure of dihydropyrimidinase from Pseudomonas aeruginosa PAO1 at 2.1 A resolution. The structure of P. aeruginosa dihydropyrimidinase reveals a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a beta-sandwich domain, which is commonly found in the architecture of dihydropyrimidinases. In contrast to all dihydropyrimidinases, P. aeruginosa dihydropyrimidinase forms a dimer, rather than a tetramer, both in the crystalline state and in the solution. Basing on sequence analysis and structural comparison of the C-terminal region and the dimer-dimer interface between P. aeruginosa dihydropyrimidinase and Thermus sp. dihydropyrimidinase, we propose a working model to explain why this enzyme cannot be a tetramer.
Crystal structure of dihydropyrimidinase from Pseudomonas aeruginosa PAO1: Insights into the molecular basis of formation of a dimer.,Tzeng CT, Huang YH, Huang CY Biochem Biophys Res Commun. 2016 Sep 23;478(3):1449-55. doi:, 10.1016/j.bbrc.2016.08.144. Epub 2016 Aug 26. PMID:27576201[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tzeng CT, Huang YH, Huang CY. Crystal structure of dihydropyrimidinase from Pseudomonas aeruginosa PAO1: Insights into the molecular basis of formation of a dimer. Biochem Biophys Res Commun. 2016 Sep 23;478(3):1449-55. doi:, 10.1016/j.bbrc.2016.08.144. Epub 2016 Aug 26. PMID:27576201 doi:http://dx.doi.org/10.1016/j.bbrc.2016.08.144
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