View source for 5uzl


==Brassica napus DGAT1 exosite==
<StructureSection load='5uzl' size='340' side='right'caption='[[5uzl]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5uzl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Brassica_napus Brassica napus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UZL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UZL FirstGlance]. <br>
</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=5uzl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uzl OCA], [https://pdbe.org/5uzl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5uzl RCSB], [https://www.ebi.ac.uk/pdbsum/5uzl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5uzl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/K9LL63_BRANA K9LL63_BRANA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Diacylglycerol acyltransferase 1 (DGAT1) is an integral membrane enzyme catalyzing the final and committed step in the acyl-coenzyme A (CoA)-dependent biosynthesis of triacylglycerol (TAG). The biochemical regulation of TAG assembly remains one of the least understood areas of primary metabolism to date. Here, we report that the hydrophilic N-terminal domain of Brassica napus DGAT1 (BnaDGAT11-113) regulates activity based on acyl-CoA/CoA levels. The N-terminal domain is not necessary for acyltransferase activity and is composed of an intrinsically disordered region and a folded segment. We show that the disordered region has an autoinhibitory function and a dimerization interface, which appears to mediate positive cooperativity, whereas the folded segment of the cytosolic region was found to have an allosteric site for acyl-CoA/CoA. Under increasing acyl-CoA levels, the binding of acyl-CoA with this noncatalytic site facilitates homotropic allosteric activation. Enzyme activation, on the other hand, is prevented under limiting acyl-CoA conditions (low acyl-CoA-to-CoA ratio), whereby CoA acts as a noncompetitive feedback inhibitor through interaction with the same folded segment. The three-dimensional NMR solution structure of the allosteric site revealed an alpha-helix with a loop connecting a coil fragment. The conserved amino acid residues in the loop interacting with CoA were identified, revealing details of this important regulatory element for allosteric regulation. Based on these results, a model is proposed illustrating the role of the N-terminal domain of BnaDGAT1 as a positive and negative modulator of TAG biosynthesis.

Diacylglycerol Acyltransferase 1 Is Regulated by Its N-Terminal Domain in Response to Allosteric Effectors.,Caldo KMP, Acedo JZ, Panigrahi R, Vederas JC, Weselake RJ, Lemieux MJ Plant Physiol. 2017 Oct;175(2):667-680. doi: 10.1104/pp.17.00934. Epub 2017 Aug, 21. PMID:28827454<ref>PMID:28827454</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5uzl" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Brassica napus]]
[[Category: Large Structures]]
[[Category: Acedo JZ]]
[[Category: Vederas JC]]