2DRY

Crystal structure of the earthworm lectin C-terminal domain mutant

2DRY の概要

• エントリーDOI: 10.2210/pdb2dry/pdb
• 関連するPDBエントリー: 2AO3 2D12 2DRZ 2DS0
• 分子名称: 29-kDa galactose-binding lectin, SULFATE ION, TRIETHYLENE GLYCOL, ... (4 entities in total)
• 機能のキーワード: earthworm lumbricus terrestris, sialic acid, galactose, in vitro evolution, beta-trefoil fold, sugar binding protein
• 由来する生物種: Lumbricus terrestris (common earthworm)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 29548.91

構造登録者

Suzuki, R.,Fujimoto, Z. (登録日: 2006-06-16, 公開日: 2007-02-06, 最終更新日: 2023-10-25)

主引用文献

Yabe, R.,Suzuki, R.,Kuno, A.,Fujimoto, Z.,Jigami, Y.,Hirabayashi, J.
Tailoring a novel sialic acid-binding lectin from a ricin-B chain-like galactose-binding protein by natural evolution-mimicry
J.Biochem., 141:389-399, 2007

PubMed Abstract: Sialic acid (Sia) is a typical terminal sugar, which modifies various types of glycoconjugates commonly found in higher animals. Its regulatory roles in diverse biological phenomena are frequently triggered by interaction with Sia-binding lectins. When using natural Sia-binding lectins as probes, however, there have been practical problems concerning their repertoire and availability. Here, we show a rational creation of a Sia-binding lectin based on the strategy 'natural evolution-mimicry', where Sia-binding lectins are engineered by error-prone PCR from a Gal-binding lectin used as a scaffold protein. After selection with fetuin-agarose using a recently reinforced ribosome display system, one of the evolved mutants SRC showed substantial affinity for alpha2-6Sia, which the parental Gal-binding lectin EW29Ch lacked. SRC was found to have additional practical advantages in productivity and in preservation of affinity for Gal. Thus, the developed novel Sia-recognition protein will contribute as useful tools to sialoglycomics.

PubMed: 17234683
DOI: 10.1093/jb/mvm043

実験手法

X-RAY DIFFRACTION (1.8 Å)