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6rkf
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of human DASPO== | |
| + | <StructureSection load='6rkf' size='340' side='right'caption='[[6rkf]], [[Resolution|resolution]] 3.22Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6rkf]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RKF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RKF FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/D-aspartate_oxidase D-aspartate oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.1 1.4.3.1] </span></td></tr> | ||
| + | <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=6rkf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rkf OCA], [http://pdbe.org/6rkf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rkf RCSB], [http://www.ebi.ac.uk/pdbsum/6rkf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rkf ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/OXDD_HUMAN OXDD_HUMAN]] Selectively catalyzes the oxidative deamination of D-aspartate and its N-methylated derivative, N-methyl D-aspartate. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | d-Amino acids are the "wrong" enantiomers of amino acids as they are not used in proteins synthesis but evolved in selected functions. On this side, d-aspartate (d-Asp) plays several significant roles in mammals, especially as an agonist of N-methyl-d-aspartate receptors (NMDAR), and is involved in relevant diseases, such as schizophrenia and Alzheimer's disease. In vivo modulation of d-Asp levels represents an intriguing task to cope with such pathological states. As little is known about d-Asp synthesis, the only option for modulating the levels is via degradation, which is due to the flavoenzyme d-aspartate oxidase (DASPO). Here we present the first three-dimensional structure of a DASPO enzyme (from human) which belongs to the d-amino acid oxidase family. Notably, human DASPO differs from human d-amino acid oxidase (attributed to d-serine degradation, the main coagonist of NMDAR) showing peculiar structural features (a specific active site charge distribution), oligomeric state and kinetic mechanism, and a higher FAD affinity and activity. These results provide useful insights into the structure-function relationships of human DASPO: modulating its activity represents now a feasible novel therapeutic target. | ||
| - | + | Structure and kinetic properties of human d-aspartate oxidase, the enzyme-controlling d-aspartate levels in brain.,Molla G, Chaves-Sanjuan A, Savinelli A, Nardini M, Pollegioni L FASEB J. 2020 Jan;34(1):1182-1197. doi: 10.1096/fj.201901703R. Epub 2019 Nov 29. PMID:31914658<ref>PMID:31914658</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6rkf" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: D-aspartate oxidase]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Chaves-Sanjuan, A]] | [[Category: Chaves-Sanjuan, A]] | ||
[[Category: Nardini, M]] | [[Category: Nardini, M]] | ||
| + | [[Category: D-aspartate]] | ||
| + | [[Category: Daspo]] | ||
| + | [[Category: Ddo]] | ||
| + | [[Category: Fad]] | ||
| + | [[Category: Flavoprotein]] | ||
| + | [[Category: Hdaspo]] | ||
| + | [[Category: Hddo oxidoreductase]] | ||
| + | [[Category: Oxidase]] | ||
Revision as of 07:25, 11 March 2020
Structure of human DASPO
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Categories: D-aspartate oxidase | Large Structures | Chaves-Sanjuan, A | Nardini, M | D-aspartate | Daspo | Ddo | Fad | Flavoprotein | Hdaspo | Hddo oxidoreductase | Oxidase
