4AL9

Crystal structure of the lectin PA-IL from Pseudomonas aeruginoas in complex with melibiose

4AL9 の概要

• エントリーDOI: 10.2210/pdb4al9/pdb
• 関連するPDBエントリー: 1L7L 1OKO 1UOJ 2VXJ 2WYF 3ZYB 3ZYF 3ZYH 4A6S
• 関連するBIRD辞書のPRD_ID: PRD_900037
• 分子名称: PA-I GALACTOPHILIC LECTIN, alpha-D-galactopyranose-(1-6)-alpha-D-glucopyranose, CALCIUM ION, ... (6 entities in total)
• 機能のキーワード: sugar binding protein, galactose binding protein
• 由来する生物種: PSEUDOMONAS AERUGINOSA
• 細胞内の位置: Cytoplasm: Q05097
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 104557.59

構造登録者

Blanchard, B.,Imberty, A.,Varrot, A. (登録日: 2012-03-02, 公開日: 2013-03-20, 最終更新日: 2023-12-20)

主引用文献

Blanchard, B.,Imberty, A.,Varrot, A.
Secondary Sugar Binding Site Identified for Leca Lectin from Pseudomonas Aeruginosa.
Proteins, 82:1060-, 2014

PubMed Abstract: The galactose-specific lectin LecA from Pseudomonas aeruginosa is a target for the development of new anti-infectious compounds. Sugar based molecules with anti-adhesive properties present great potential in the fight against bacterial infection and biofilm formation. LecA is specific for oligosaccharides with terminal α-galactoside residues and displays strong affinity for melibiose (αGal1-6Glc) with a Kd of 38.8 µM. The crystal structure of LecA/melibiose complex shows classical calcium-bridged binding of αGal in the primary binding site but also revealed a secondary sugar binding site with glucose bound. This sugar binding site is in close proximity to the galactose binding one, is independent of calcium and mainly involves interactions with a symmetry-related protein. This discovery would help to the design of new potent inhibitors targeting both binding sites.

PubMed: 24123124
DOI: 10.1002/PROT.24430

実験手法

X-RAY DIFFRACTION (1.75 Å)