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| | ==Biophysical studies of lipid interacting regions of DGD2 in Arabidopsis thaliana== | | ==Biophysical studies of lipid interacting regions of DGD2 in Arabidopsis thaliana== |
| - | <StructureSection load='2l7c' size='340' side='right' caption='[[2l7c]], [[NMR_Ensembles_of_Models | 23 NMR models]]' scene=''> | + | <StructureSection load='2l7c' size='340' side='right'caption='[[2l7c]], [[NMR_Ensembles_of_Models | 23 NMR models]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2l7c]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L7C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L7C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2l7c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arath Arath]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L7C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L7C FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1z2t|1z2t]]</td></tr> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1z2t|1z2t]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DGD2, At4g00550, F6N23.24 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DGD2, At4g00550, F6N23.24 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Digalactosyldiacylglycerol_synthase Digalactosyldiacylglycerol synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.241 2.4.1.241] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Digalactosyldiacylglycerol_synthase Digalactosyldiacylglycerol synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.241 2.4.1.241] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2l7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l7c OCA], [http://pdbe.org/2l7c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l7c RCSB], [http://www.ebi.ac.uk/pdbsum/2l7c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2l7c ProSAT]</span></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=2l7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l7c OCA], [https://pdbe.org/2l7c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l7c RCSB], [https://www.ebi.ac.uk/pdbsum/2l7c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l7c ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DGDG2_ARATH DGDG2_ARATH]] Involved in the synthesis of diacylglycerol galactolipids that are specifically found in thylakoid membranes. Specific for alpha-glycosidic linkages.<ref>PMID:11696551</ref> <ref>PMID:14600212</ref> | + | [[https://www.uniprot.org/uniprot/DGDG2_ARATH DGDG2_ARATH]] Involved in the synthesis of diacylglycerol galactolipids that are specifically found in thylakoid membranes. Specific for alpha-glycosidic linkages.<ref>PMID:11696551</ref> <ref>PMID:14600212</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | [[Category: Arath]] | | [[Category: Arath]] |
| | [[Category: Digalactosyldiacylglycerol synthase]] | | [[Category: Digalactosyldiacylglycerol synthase]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Ge, C]] | | [[Category: Ge, C]] |
| | [[Category: Iakovleva, I]] | | [[Category: Iakovleva, I]] |
| Structural highlights
Function
[DGDG2_ARATH] Involved in the synthesis of diacylglycerol galactolipids that are specifically found in thylakoid membranes. Specific for alpha-glycosidic linkages.[1] [2]
Publication Abstract from PubMed
Membrane lipid glycosyltransferases (GTs) in plants are enzymes that regulate the levels of the non-bilayer prone monogalactosyldiacylglycerol (GalDAG) and the bilayer-forming digalactosyldiacylglycerol (GalGalDAG). The relative amounts of these lipids affect membrane properties such as curvature and lateral stress. During phosphate shortage, phosphate is rescued by replacing phospholipids with GalGalDAG. The glycolsyltransferase enzyme in Arabidopsis thaliana responsible for this, atDGD2, senses the bilayer properties and interacts with the membrane in a monotopic manner. To understand the parameters that govern this interaction, we have identified several possible lipid-interacting sites in the protein and studied these by biophysical techniques. We have developed a multivariate discrimination algorithm that correctly predicts the regions in the protein that interact with lipids, and the interactions were confirmed by a variety of biophysical techniques. We show by bioinformatic methods and circular dichroism (CD), fluorescence, and NMR spectroscopic techniques that two regions are prone to interact with lipids in a surface-charge dependent way. Both of these regions contain Trp residues, but here charge appears to be the dominating feature governing the interaction. The sequence corresponding to residues 227-245 in the protein is seen to be able to adapt its structure according to the surface-charge density of a bilayer. All results indicate that this region interacts specifically with lipid molecules and that a second region in the protein, corresponding to residues 130-148, also interacts with the bilayer. On the basis of this, and sequence charge features in the immediate environment of S227-245, a response model for the interaction of atDGD2 with the membrane bilayer interface is proposed.
Lipid interacting regions in phosphate stress glycosyltransferase atDGD2 from Arabidopsis thaliana.,Szpryngiel S, Ge C, Iakovleva I, Georgiev A, Lind J, Wieslander A, Maler L Biochemistry. 2011 May 31;50(21):4451-66. Epub 2011 May 4. PMID:21506606[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kelly AA, Dormann P. DGD2, an arabidopsis gene encoding a UDP-galactose-dependent digalactosyldiacylglycerol synthase is expressed during growth under phosphate-limiting conditions. J Biol Chem. 2002 Jan 11;277(2):1166-73. Epub 2001 Nov 5. PMID:11696551 doi:http://dx.doi.org/10.1074/jbc.M110066200
- ↑ Kelly AA, Froehlich JE, Dormann P. Disruption of the two digalactosyldiacylglycerol synthase genes DGD1 and DGD2 in Arabidopsis reveals the existence of an additional enzyme of galactolipid synthesis. Plant Cell. 2003 Nov;15(11):2694-706. PMID:14600212 doi:http://dx.doi.org/10.1105/tpc016675
- ↑ Szpryngiel S, Ge C, Iakovleva I, Georgiev A, Lind J, Wieslander A, Maler L. Lipid interacting regions in phosphate stress glycosyltransferase atDGD2 from Arabidopsis thaliana. Biochemistry. 2011 May 31;50(21):4451-66. Epub 2011 May 4. PMID:21506606 doi:10.1021/bi200162f
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