3ZI8

Structure of the R17A mutant of the Ralstonia soleanacerum lectin at 1.5 Angstrom in complex with L-fucose

3ZI8 の概要

• エントリーDOI: 10.2210/pdb3zi8/pdb
• 分子名称: PUTATIVE FUCOSE-BINDING LECTIN PROTEIN, beta-L-fucopyranose, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: sugar binding protein, multivalency
• 由来する生物種: RALSTONIA SOLANACEARUM
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9954.08

構造登録者

Arnaud, J.,Audfray, A.,Claudinon, J.,Trondle, K.,Trosvalet, M.,Thomas, A.,Varrot, A.,Romer, W.,Imberty, A. (登録日: 2013-01-07, 公開日: 2013-07-31, 最終更新日: 2023-12-20)

主引用文献

Arnaud, J.,Claudinon, J.,Trondle, K.,Trovaslet, M.,Larson, G.,Thomas, A.,Varrot, A.,Romer, W.,Imberty, A.,Audfray, A.
Reduction of Lectin Valency Drastically Changes Glycolipid Dynamics in Membranes, But not Surface Avidity.
Acs Chem.Biol., 8:1918-, 2013

PubMed Abstract: Multivalency is proposed to play a role in the strong avidity of lectins for glycosylated cell surfaces and also in their ability to affect membrane dynamics by clustering glycosphingolipids. Lectins with modified valency were designed from the β-propeller fold of Ralstonia solanacearum lectin (RSL) that presents six fucose binding sites. After identification of key amino acids by molecular dynamics calculations, two mutants with reduced valency were produced. Isothermal titration calorimetry confirmed the loss of three high affinity binding sites for both mutants. Crystal structures indicated that residual low affinity binding occurred in W76A but not in R17A. The trivalent R17A mutant presented unchanged avidity toward fucosylated surfaces, when compared to hexavalent RSL. However, R17A is not able anymore to induce formation of membrane invaginations on giant unilamellar vesicules, indicating the crucial role of number of binding sites for clustering of glycolipids. In the human lung epithelial cell line H1299, wt-RSL is internalized within seconds whereas the kinetics of R17A uptake is largely delayed. Neolectins with tailored valency are promising tools to study membrane dynamics.

PubMed: 23855446
DOI: 10.1021/CB400254B

実験手法

X-RAY DIFFRACTION (1.5 Å)