View source for 4bca


==MAMMALIAN ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE: Tyr578Phe mutant==
<StructureSection load='4bca' size='340' side='right'caption='[[4bca]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4bca]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Cavia_porcellus Cavia porcellus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BCA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BCA FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4bca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bca OCA], [https://pdbe.org/4bca PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bca RCSB], [https://www.ebi.ac.uk/pdbsum/4bca PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bca ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ADAS_CAVPO ADAS_CAVPO] 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.<ref>PMID:23112191</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The precursor of the essential ether phospholipids is synthesized by a peroxisomal enzyme that uses a flavin cofactor to catalyze a reaction that does not alter the redox state of the substrates. The enzyme crystal structure reveals a V-shaped active site with a narrow constriction in front of the prosthetic group. Mutations causing inborn ether phospholipid deficiency, a very severe genetic disease, target residues that are part of the catalytic center. Biochemical analysis using substrate and flavin analogs, absorbance spectroscopy, mutagenesis, and mass spectrometry provide compelling evidence supporting an unusual mechanism of covalent catalysis. The flavin functions as a chemical trap that promotes exchange of an acyl with an alkyl group, generating the characteristic ether bond. Structural comparisons show that the covalent versus noncovalent mechanistic distinction in flavoenzyme catalysis and evolution relies on subtle factors rather than on gross modifications of the cofactor environment.

Precursor of ether phospholipids is synthesized by a flavoenzyme through covalent catalysis.,Nenci S, Piano V, Rosati S, Aliverti A, Pandini V, Fraaije MW, Heck AJ, Edmondson DE, Mattevi A Proc Natl Acad Sci U S A. 2012 Nov 13;109(46):18791-6. doi:, 10.1073/pnas.1215128109. Epub 2012 Oct 29. PMID:23112191<ref>PMID:23112191</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4bca" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Cavia porcellus]]
[[Category: Large Structures]]
[[Category: Aliverti A]]
[[Category: Edmondson DE]]
[[Category: Fraaije MW]]
[[Category: Heck AJR]]
[[Category: Mattevi A]]
[[Category: Nenci S]]
[[Category: Pandini V]]
[[Category: Piano V]]
[[Category: Rosati S]]