6rkf: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 6rkf is ~~ON HOLD until Paper~~ Publication

==Structure of human DASPO==

== 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.

== 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.

~~Authors:~~ Chaves-Sanjuan, A., Nardini, M.

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>

~~Description~~: ~~Structure of human DASPO~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased~~ Structures]]

</div>

== References ==

__TOC__

</StructureSection>

[[Category: D-aspartate oxidase]]

[[Category: Large Structures]]

[[Category: Chaves-Sanjuan, A]]

[[Category: Nardini, M]]

[[Category: D-aspartate]]

[[Category: Daspo]]

[[Category: Ddo]]

[[Category: Fad]]

[[Category: Flavoprotein]]

[[Category: Hdaspo]]

[[Category: Hddo oxidoreductase]]

[[Category: Oxidase]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6rkf is ON HOLD  until Paper Publication
+==Structure of human DASPO==
+<StructureSection load='6rkf' size='340' side='right'caption='[[6rkf]], [[Resolution|resolution]] 3.22&Aring;' 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.
-Authors: Chaves-Sanjuan, A., Nardini, M.
+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>
-Description: Structure of human DASPO
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</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: Nardini, M]]
+[[Category: D-aspartate]]
+[[Category: Daspo]]
+[[Category: Ddo]]
+[[Category: Fad]]
+[[Category: Flavoprotein]]
+[[Category: Hdaspo]]
+[[Category: Hddo oxidoreductase]]
+[[Category: Oxidase]]