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| | ==Crystal Structure of Dihydropteridine Reductase from Dictyostelium discoideum== | | ==Crystal Structure of Dihydropteridine Reductase from Dictyostelium discoideum== |
| - | <StructureSection load='3orf' size='340' side='right' caption='[[3orf]], [[Resolution|resolution]] 2.16Å' scene=''> | + | <StructureSection load='3orf' size='340' side='right'caption='[[3orf]], [[Resolution|resolution]] 2.16Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3orf]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ORF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ORF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3orf]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ORF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ORF FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</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]] 2.16Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ooe|1ooe]], [[1hdr|1hdr]], [[1dir|1dir]], [[1dhr|1dhr]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DDB_G0272684, qdpr ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=44689 Dictyostelium discoideum])</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=3orf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3orf OCA], [https://pdbe.org/3orf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3orf RCSB], [https://www.ebi.ac.uk/pdbsum/3orf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3orf 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/6,7-dihydropteridine_reductase 6,7-dihydropteridine reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.34 1.5.1.34] </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=3orf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3orf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3orf RCSB], [http://www.ebi.ac.uk/pdbsum/3orf PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DHPR_DICDI DHPR_DICDI]] The product of this enzyme, tetrahydrobiopterin (BH-4), is an essential cofactor for phenylalanine, tyrosine, and tryptophan hydroxylases (By similarity). | + | [https://www.uniprot.org/uniprot/DHPR_DICDI DHPR_DICDI] The product of this enzyme, tetrahydrobiopterin (BH-4), is an essential cofactor for phenylalanine, tyrosine, and tryptophan hydroxylases (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 3orf" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 6,7-dihydropteridine reductase]] | |
| | [[Category: Dictyostelium discoideum]] | | [[Category: Dictyostelium discoideum]] |
| - | [[Category: Chen, C]] | + | [[Category: Large Structures]] |
| - | [[Category: Lee, K H]] | + | [[Category: Chen C]] |
| - | [[Category: Park, Y S]] | + | [[Category: Lee KH]] |
| - | [[Category: Seo, K H]] | + | [[Category: Park YS]] |
| - | [[Category: Zhuang, N N]] | + | [[Category: Seo KH]] |
| - | [[Category: Alpha-beta-alpha sandwich]] | + | [[Category: Zhuang NN]] |
| - | [[Category: Nadh binding]]
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| - | [[Category: Oxidoreductase]]
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| - | [[Category: Rossmann fold]]
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| Structural highlights
Function
DHPR_DICDI The product of this enzyme, tetrahydrobiopterin (BH-4), is an essential cofactor for phenylalanine, tyrosine, and tryptophan hydroxylases (By similarity).
Publication Abstract from PubMed
Up to now, d-threo-tetrahydrobiopterin (DH(4), dictyopterin) was detected only in Dictyostelium discoideum, while the isomer l-erythro-tetrahydrobioterin (BH(4)) is common in mammals. To elucidate the mechanism of DH(4) regeneration by D. discoideum dihydropteridine reductase (DicDHPR), we have determined the crystal structure of DicDHPR complexed with NAD(+) at 2.16A resolution. Significant structural differences from mammalian DHPRs are found around the coenzyme binding site, resulting in a higher K(m) value for NADH (K(m)=46.51+/-0.4muM) than mammals. In addition, we have found that rat DHPR as well as DicDHPR could bind to both substrates quinonoid-BH(2) and quinonoid-DH(2) by docking calculations and have confirmed their catalytic activity by in vitro assay. STRUCTURED SUMMARY OF PROTEIN INTERACTIONS: DHPRbindstoDHPR by X-ray crystallography(View interaction).
Structural insights into the dual substrate specificities of mammalian and Dictyostelium dihydropteridine reductases toward two stereoisomers of quinonoid dihydrobiopterin.,Chen C, Kim HL, Zhuang N, Seo KH, Park KH, Han CD, Park YS, Lee KH FEBS Lett. 2011 Sep 2;585(17):2640-6. Epub 2011 Jul 30. PMID:21819985[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chen C, Kim HL, Zhuang N, Seo KH, Park KH, Han CD, Park YS, Lee KH. Structural insights into the dual substrate specificities of mammalian and Dictyostelium dihydropteridine reductases toward two stereoisomers of quinonoid dihydrobiopterin. FEBS Lett. 2011 Sep 2;585(17):2640-6. Epub 2011 Jul 30. PMID:21819985 doi:10.1016/j.febslet.2011.07.018
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