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| | <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 [https://en.wikipedia.org/wiki/Dicdi Dicdi]. 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> | + | <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" id="ligandDat"><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"><div style='overflow: auto; max-height: 3em;'>[[1ooe|1ooe]], [[1hdr|1hdr]], [[1dir|1dir]], [[1dhr|1dhr]]</div></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 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=44689 DICDI])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/6,7-dihydropteridine_reductase 6,7-dihydropteridine reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.34 1.5.1.34] </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=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='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> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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).
| + | [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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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 6,7-dihydropteridine reductase]] | + | [[Category: Dictyostelium discoideum]] |
| - | [[Category: Dicdi]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chen, C]] | + | [[Category: Chen C]] |
| - | [[Category: Lee, K H]] | + | [[Category: Lee KH]] |
| - | [[Category: Park, Y S]] | + | [[Category: Park YS]] |
| - | [[Category: Seo, K H]] | + | [[Category: Seo KH]] |
| - | [[Category: Zhuang, N N]] | + | [[Category: Zhuang NN]] |
| - | [[Category: Alpha-beta-alpha sandwich]]
| + | |
| - | [[Category: Nadh binding]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Rossmann fold]]
| + | |
| 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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