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| | <StructureSection load='2uuu' size='340' side='right'caption='[[2uuu]], [[Resolution|resolution]] 1.95Å' scene=''> | | <StructureSection load='2uuu' size='340' side='right'caption='[[2uuu]], [[Resolution|resolution]] 1.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2uuu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_11735 Atcc 11735]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UUU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2UUU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2uuu]] 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=2UUU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2UUU FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PL3:HEXADECAN-1-OL'>PL3</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]] 1.95Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2uuv|2uuv]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PL3:HEXADECAN-1-OL'>PL3</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Alkylglycerone-phosphate_synthase Alkylglycerone-phosphate synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.26 2.5.1.26] </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=2uuu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uuu OCA], [https://pdbe.org/2uuu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2uuu RCSB], [https://www.ebi.ac.uk/pdbsum/2uuu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2uuu 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=2uuu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uuu OCA], [https://pdbe.org/2uuu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2uuu RCSB], [https://www.ebi.ac.uk/pdbsum/2uuu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2uuu ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/ADAS_DICDI ADAS_DICDI]] Catalyzes the exchange of an acyl for a long-chain alkyl group and the formation of the ether bond in the biosynthesis of ether phospholipids.
| + | [https://www.uniprot.org/uniprot/ADAS_DICDI ADAS_DICDI] Catalyzes the exchange of an acyl for a long-chain alkyl group and the formation of the ether bond in the biosynthesis of ether phospholipids. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Alkylglycerone-phosphate synthase]] | + | [[Category: Dictyostelium discoideum]] |
| - | [[Category: Atcc 11735]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Aliverti, A]] | + | [[Category: Aliverti A]] |
| - | [[Category: Carpanelli, E]] | + | [[Category: Carpanelli E]] |
| - | [[Category: Coda, A]] | + | [[Category: Coda A]] |
| - | [[Category: Mattevi, A]] | + | [[Category: Mattevi A]] |
| - | [[Category: Mattiroli, F]] | + | [[Category: Mattiroli F]] |
| - | [[Category: Pandini, V]] | + | [[Category: Pandini V]] |
| - | [[Category: Razeto, A]] | + | [[Category: Razeto A]] |
| - | [[Category: Lavoprotein]]
| + | |
| - | [[Category: Lipid synthesis]]
| + | |
| - | [[Category: Peroxisomal disorder]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
ADAS_DICDI Catalyzes the exchange of an acyl for a long-chain alkyl group and the formation of the ether bond in the biosynthesis of ether phospholipids.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Ether phospholipids are essential constituents of eukaryotic cell membranes. Rhizomelic chondrodysplasia punctata type 3 is a severe peroxisomal disorder caused by inborn deficiency of alkyldihydroxyacetonephosphate synthase (ADPS). The enzyme carries out the most characteristic step in ether phospholipid biosynthesis: formation of the ether bond. The crystal structure of ADPS from Dictyostelium discoideum shows a fatty-alcohol molecule bound in a narrow hydrophobic tunnel, specific for aliphatic chains of 16 carbons. Access to the tunnel is controlled by a flexible loop and a gating helix at the protein-membrane interface. Structural and mutagenesis investigations identify a cluster of hydrophilic catalytic residues, including an essential tyrosine, possibly involved in substrate proton abstraction, and the arginine that is mutated in ADPS-deficient patients. We propose that ether bond formation might be orchestrated through a covalent imine intermediate with the flavin, accounting for the noncanonical employment of a flavin cofactor in a nonredox reaction.
The crucial step in ether phospholipid biosynthesis: structural basis of a noncanonical reaction associated with a peroxisomal disorder.,Razeto A, Mattiroli F, Carpanelli E, Aliverti A, Pandini V, Coda A, Mattevi A Structure. 2007 Jun;15(6):683-92. PMID:17562315[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Razeto A, Mattiroli F, Carpanelli E, Aliverti A, Pandini V, Coda A, Mattevi A. The crucial step in ether phospholipid biosynthesis: structural basis of a noncanonical reaction associated with a peroxisomal disorder. Structure. 2007 Jun;15(6):683-92. PMID:17562315 doi:10.1016/j.str.2007.04.009
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