3orf
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of Dihydropteridine Reductase from Dictyostelium discoideum== | |
| + | <StructureSection load='3orf' size='340' side='right'caption='[[3orf]], [[Resolution|resolution]] 2.16Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <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='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='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='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> | ||
| + | == 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). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:21819985</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3orf" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Dictyostelium discoideum]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Chen C]] | ||
| + | [[Category: Lee KH]] | ||
| + | [[Category: Park YS]] | ||
| + | [[Category: Seo KH]] | ||
| + | [[Category: Zhuang NN]] | ||
Current revision
Crystal Structure of Dihydropteridine Reductase from Dictyostelium discoideum
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