2L7C

Biophysical studies of lipid interacting regions of DGD2 in Arabidopsis thaliana

2L7C の概要

• エントリーDOI: 10.2210/pdb2l7c/pdb
• 関連するPDBエントリー: 1Z2T
• NMR情報: BMRB: 17356
• 分子名称: Digalactosyldiacylglycerol synthase 2, chloroplastic (1 entity in total)
• 機能のキーワード: amphipathic helix, glycosyltransferase, dgdg, diglycosyldiacylglycerol, transferase
• 由来する生物種: Arabidopsis thaliana (mouse-ear cress,thale-cress)
• 細胞内の位置: Plastid, chloroplast outer membrane: Q8W1S1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2227.60

構造登録者

Szpryngiel, S.,Ge, C.,Iakovleva, I.,Lind, J.,Wieslander, A.,Maler, L. (登録日: 2010-12-07, 公開日: 2011-10-19, 最終更新日: 2024-05-22)

主引用文献

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, 50:4451-4466, 2011

PubMed Abstract: 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.

PubMed: 21506606
DOI: 10.1021/bi200162f

実験手法

SOLUTION NMR