7x0c: Difference between revisions
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==Crystal structure of phospholipase A1, AtDSEL== | |||
<StructureSection load='7x0c' size='340' side='right'caption='[[7x0c]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7x0c]] 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=7X0C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7X0C 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]] 1.7990952Å</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=7x0c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7x0c OCA], [https://pdbe.org/7x0c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7x0c RCSB], [https://www.ebi.ac.uk/pdbsum/7x0c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7x0c ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/DSEL_ARATH DSEL_ARATH] Acylhydrolase that catalyzes the hydrolysis of 1,3-diacylglycerol (1,3-DAG) and 1-monoacylglycerol (1-MAG) at the sn-1 position. High activity toward 1,3-DAG and 1-MAG, but low activity toward 1,2-diacylglycerol (1,2-DAG) and 1-lysophosphatidylcholine (1-LPC), and no activity toward phosphatidylcholine (PC), monogalactosyldiacylglycerol (MGDG), digalactosyldiacylglycerol (DGDG), triacylglycerol (TAG) and 2-monoacylglycerol (2-MAG). May be involved in the negative regulation of seedling establishment by inhibiting the breakdown, beta-oxidation and mobilization of seed storage oils. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Phospholipase is an enzyme that hydrolyzes various phospholipid substrates at specific ester bonds and plays important roles such as membrane remodeling, as digestive enzymes, and the regulation of cellular mechanism. Phospholipase proteins are divided into following the four major groups according to the ester bonds they cleave off: phospholipase A1 (PLA1), phospholipase A2 (PLA2), phospholipase C (PLC), and phospholipase D (PLD). Among the four phospholipase groups, PLA1 has been less studied than the other phospholipases. Here, we report the first molecular structures of plant PLA1s: AtDSEL and CaPLA1 derived from Arabidopsis thaliana and Capsicum annuum, respectively. AtDSEL and CaPLA1 are novel PLA1s in that they form homodimers since PLAs are generally in the form of a monomer. The dimerization domain at the C-terminal of the AtDSEL and CaPLA1 makes hydrophobic interactions between each monomer, respectively. The C-terminal domain is also present in PLA1s of other plants, but not in PLAs of mammals and fungi. An activity assay of AtDSEL toward various lipid substrates demonstrates that AtDSEL is specialized for the cleavage of sn-1 acyl chains. This report reveals a new domain that exists only in plant PLA1s and suggests that the domain is essential for homodimerization. | |||
Crystal Structures of the Plant Phospholipase A1 Proteins Reveal a Unique Dimerization Domain.,Heo Y, Lee I, Moon S, Yun JH, Kim EY, Park SY, Park JH, Kim WT, Lee W Molecules. 2022 Apr 2;27(7). pii: molecules27072317. doi:, 10.3390/molecules27072317. PMID:35408716<ref>PMID:35408716</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7x0c" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: Lee | *[[Phospholipase A1|Phospholipase A1]] | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Arabidopsis thaliana]] | |||
[[Category: Large Structures]] | |||
[[Category: Heo Y]] | |||
[[Category: Lee I]] | |||
[[Category: Lee W]] | |||
[[Category: Moon S]] | |||
Latest revision as of 20:46, 29 November 2023
Crystal structure of phospholipase A1, AtDSELCrystal structure of phospholipase A1, AtDSEL
Structural highlights
FunctionDSEL_ARATH Acylhydrolase that catalyzes the hydrolysis of 1,3-diacylglycerol (1,3-DAG) and 1-monoacylglycerol (1-MAG) at the sn-1 position. High activity toward 1,3-DAG and 1-MAG, but low activity toward 1,2-diacylglycerol (1,2-DAG) and 1-lysophosphatidylcholine (1-LPC), and no activity toward phosphatidylcholine (PC), monogalactosyldiacylglycerol (MGDG), digalactosyldiacylglycerol (DGDG), triacylglycerol (TAG) and 2-monoacylglycerol (2-MAG). May be involved in the negative regulation of seedling establishment by inhibiting the breakdown, beta-oxidation and mobilization of seed storage oils. Publication Abstract from PubMedPhospholipase is an enzyme that hydrolyzes various phospholipid substrates at specific ester bonds and plays important roles such as membrane remodeling, as digestive enzymes, and the regulation of cellular mechanism. Phospholipase proteins are divided into following the four major groups according to the ester bonds they cleave off: phospholipase A1 (PLA1), phospholipase A2 (PLA2), phospholipase C (PLC), and phospholipase D (PLD). Among the four phospholipase groups, PLA1 has been less studied than the other phospholipases. Here, we report the first molecular structures of plant PLA1s: AtDSEL and CaPLA1 derived from Arabidopsis thaliana and Capsicum annuum, respectively. AtDSEL and CaPLA1 are novel PLA1s in that they form homodimers since PLAs are generally in the form of a monomer. The dimerization domain at the C-terminal of the AtDSEL and CaPLA1 makes hydrophobic interactions between each monomer, respectively. The C-terminal domain is also present in PLA1s of other plants, but not in PLAs of mammals and fungi. An activity assay of AtDSEL toward various lipid substrates demonstrates that AtDSEL is specialized for the cleavage of sn-1 acyl chains. This report reveals a new domain that exists only in plant PLA1s and suggests that the domain is essential for homodimerization. Crystal Structures of the Plant Phospholipase A1 Proteins Reveal a Unique Dimerization Domain.,Heo Y, Lee I, Moon S, Yun JH, Kim EY, Park SY, Park JH, Kim WT, Lee W Molecules. 2022 Apr 2;27(7). pii: molecules27072317. doi:, 10.3390/molecules27072317. PMID:35408716[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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