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2uuv

From Proteopedia

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[[Image:2uuv.png|left|200px]]
 
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==alkyldihydroxyacetonephosphate synthase in P1==
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The line below this paragraph, containing "STRUCTURE_2uuv", creates the "Structure Box" on the page.
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<StructureSection load='2uuv' size='340' side='right'caption='[[2uuv]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2uuv]] 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=2UUV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2UUV FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.99&#8491;</td></tr>
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<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>
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{{STRUCTURE_2uuv| PDB=2uuv | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2uuv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uuv OCA], [https://pdbe.org/2uuv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2uuv RCSB], [https://www.ebi.ac.uk/pdbsum/2uuv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2uuv ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uu/2uuv_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2uuv ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE IN P1===
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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<ref>PMID:17562315</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_17562315}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2uuv" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 17562315 is the PubMed ID number.
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== References ==
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-->
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<references/>
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{{ABSTRACT_PUBMED_17562315}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[2uuv]] 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=2UUV OCA].
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==Reference==
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<ref group="xtra">PMID:017562315</ref><references group="xtra"/>
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[[Category: Alkylglycerone-phosphate synthase]]
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[[Category: Dictyostelium discoideum]]
[[Category: Dictyostelium discoideum]]
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[[Category: Aliverti, A.]]
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[[Category: Large Structures]]
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[[Category: Carpanelli, E.]]
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[[Category: Aliverti A]]
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[[Category: Coda, A.]]
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[[Category: Carpanelli E]]
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[[Category: Mattevi, A.]]
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[[Category: Coda A]]
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[[Category: Mattiroli, F.]]
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[[Category: Mattevi A]]
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[[Category: Pandini, V.]]
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[[Category: Mattiroli F]]
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[[Category: Razeto, A.]]
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[[Category: Pandini V]]
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[[Category: Biosynthesis of phospholipid]]
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[[Category: Razeto A]]
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[[Category: Fad]]
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[[Category: Flavin]]
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[[Category: Flavoprotein]]
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[[Category: Lipid synthesis]]
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[[Category: Peroxisomal disorder]]
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[[Category: Peroxisome]]
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[[Category: Plasmalogen]]
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[[Category: Rhizomelic chondrodysplasia punctata]]
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[[Category: Transferase]]
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Current revision

alkyldihydroxyacetonephosphate synthase in P1

PDB ID 2uuv

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