3orf
From Proteopedia
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- | [[ | + | ==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 [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> | ||
+ | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene><br> | ||
+ | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ooe|1ooe]], [[1hdr|1hdr]], [[1dir|1dir]], [[1dhr|1dhr]]</td></tr> | ||
+ | <tr><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><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> | ||
+ | <tr><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> | ||
+ | <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> | |
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- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
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- | == | + | |
- | < | + | |
[[Category: 6,7-dihydropteridine reductase]] | [[Category: 6,7-dihydropteridine reductase]] | ||
[[Category: Dictyostelium discoideum]] | [[Category: Dictyostelium discoideum]] |
Revision as of 10:44, 28 May 2014
Crystal Structure of Dihydropteridine Reductase from Dictyostelium discoideum
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