2WKK

Identification of the glycan target of the nematotoxic fungal galectin CGL2 in Caenorhabditis elegans

2WKK の概要

• エントリーDOI: 10.2210/pdb2wkk/pdb
• 関連するPDBエントリー: 1UL9 1ULC 1ULD 1ULE 1ULF 1ULG
• 分子名称: GALECTIN-2, beta-D-galactopyranose-(1-4)-alpha-L-fucopyranose, beta-D-galactopyranose-(1-4)-alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
• 機能のキーワード: sugar-binding protein, lectin, galectin, secreted, cell wall, sugar binding, sugar binding protein, beta-galactoside binding lectin, fruiting body, extracellular matrix
• 由来する生物種: COPRINOPSIS CINEREA
• 細胞内の位置: Secreted, extracellular space, extracellular matrix : Q9P4R8
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 68895.77

構造登録者

Butschi, A.,Titz, A.,Waelti, M.,Olieric, V.,Paschinger, K.,Xiaoqiang, G.,Seeberger, P.H.,Wilson, I.B.H.,Aebi, M.,Hengartner, M.O.,Kuenzler, M. (登録日: 2009-06-14, 公開日: 2010-01-19, 最終更新日: 2023-12-13)

主引用文献

Butschi, A.,Titz, A.,Walti, M.A.,Olieric, V.,Paschinger, K.,Nobauer, K.,Guo, X.,Seeberger, P.H.,Wilson, I.B.H.,Aebi, M.,Hengartner, M.O.,Kunzler, M.
Caenorhabditis Elegans N-Glycan Core Beta-Galactoside Confers Sensitivity Towards Nematotoxic Fungal Galectin Cgl2.
Plos Pathog., 6:E717-, 2010

PubMed Abstract: The physiological role of fungal galectins has remained elusive. Here, we show that feeding of a mushroom galectin, Coprinopsis cinerea CGL2, to Caenorhabditis elegans inhibited development and reproduction and ultimately resulted in killing of this nematode. The lack of toxicity of a carbohydrate-binding defective CGL2 variant and the resistance of a C. elegans mutant defective in GDP-fucose biosynthesis suggested that CGL2-mediated nematotoxicity depends on the interaction between the galectin and a fucose-containing glycoconjugate. A screen for CGL2-resistant worm mutants identified this glycoconjugate as a Galbeta1,4Fucalpha1,6 modification of C. elegans N-glycan cores. Analysis of N-glycan structures in wild type and CGL2-resistant nematodes confirmed this finding and allowed the identification of a novel putative glycosyltransferase required for the biosynthesis of this glycoepitope. The X-ray crystal structure of a complex between CGL2 and the Galbeta1,4Fucalpha1,6GlcNAc trisaccharide at 1.5 A resolution revealed the biophysical basis for this interaction. Our results suggest that fungal galectins play a role in the defense of fungi against predators by binding to specific glycoconjugates of these organisms.

PubMed: 20062796
DOI: 10.1371/JOURNAL.PPAT.1000717

実験手法

X-RAY DIFFRACTION (1.5 Å)