9vk0
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of plant diacylglycerol O-acyltransferase 1== | |
| + | <StructureSection load='9vk0' size='340' side='right'caption='[[9vk0]], [[Resolution|resolution]] 3.01Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9vk0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9VK0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9VK0 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.01Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1LVF:2,3-bis[[(~{Z})-octadec-9-enoyl]oxy]propyl+(~{Z})-octadec-9-enoate'>A1LVF</scene>, <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</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=9vk0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9vk0 OCA], [https://pdbe.org/9vk0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9vk0 RCSB], [https://www.ebi.ac.uk/pdbsum/9vk0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9vk0 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/DGAT1_ARATH DGAT1_ARATH] Major contributor to triacylglycerol (TAG) synthesis and oil accumulation in seeds. Catalyzes the acylation of the sn-3 hydroxy group of sn-1,2-diacylglycerol using acyl-CoA (PubMed:10571850, PubMed:10580283, PubMed:10601854, PubMed:11402213, PubMed:12114588, PubMed:20040537, PubMed:20101470). Can use palmitoyl-CoA and oleoyl-CoA as substrates (PubMed:20101470). Can use oleoyl-CoA and linoleoyl-CoA as substrates. Has substrate preference for oleoyl-CoA compared to linoleoyl-CoA (PubMed:23770095). Has complementary functions with PDAT1 that are essential for triacylglycerol synthesis and normal development of both seeds and pollen (PubMed:20040537).<ref>PMID:10571850</ref> <ref>PMID:10580283</ref> <ref>PMID:10601854</ref> <ref>PMID:11402213</ref> <ref>PMID:12114588</ref> <ref>PMID:20040537</ref> <ref>PMID:20101470</ref> <ref>PMID:23770095</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Triacylglycerol (TAG) constitutes the primary component of plant oils and is essential for food and biodiesel production. Diacylglycerol O-acyltransferase-1 (DGAT1), the key rate-limiting enzyme in TAG biosynthesis, is an important target for engineering plants with enhanced oil yield and improved fatty acyl composition. Environmental stress triggers the accumulation of toxic lipid intermediates such as free fatty acids (FFAs) and diacylglycerols (DAGs). Plants alleviate lipid toxicity by upregulating DGAT1 to channel the intermediates into TAG. Through biochemical studies, we demonstrate that FFAs directly enhance the activity of Arabidopsis (Arabidopsis thaliana) DGAT1 (AtDGAT1) by approximately 3-fold. Cryo-electron microscopy structures of wild-type (WT) AtDGAT1 and a low-activity mutant (H447A) reveal the binding sites for both substrates (DAG and oleoyl-CoA), 2 products (TAG and CoASH), and multiple FFA molecules. Remarkably, mutating a cysteine residue (Cys246) in contact with the FFA head group to Ala, Ser, or Thr increases AtDAGT1 activity significantly. The C246A mutant accommodates the carboxyl group of FFA slightly deeper within the active site, potentially enhancing substrate binding. Furthermore, the FFA molecules orient the acyl-CoA tail at a position favorable for the catalytic reaction. Our integrated biochemical and structural results provide insights into the catalytic mechanism and activity regulation of DGAT1, which will enable the future engineering of oil crops. | ||
| - | + | Structural mechanisms underlying the free fatty acid-mediated regulation of DIACYLGLYCEROL O-ACYLTRANSFERASE 1 in Arabidopsis.,Liu X, Li J, Song D, Liu Z Plant Cell. 2025 Oct 8;37(10):koaf239. doi: 10.1093/plcell/koaf239. PMID:41081525<ref>PMID:41081525</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 9vk0" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Arabidopsis thaliana]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Li JJ]] | ||
| + | [[Category: Liu XY]] | ||
| + | [[Category: Liu ZF]] | ||
| + | [[Category: Song DF]] | ||
Current revision
Structure of plant diacylglycerol O-acyltransferase 1
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