4AL9

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

Summary for 4AL9

• Entry DOI: 10.2210/pdb4al9/pdb
• Related: 1L7L 1OKO 1UOJ 2VXJ 2WYF 3ZYB 3ZYF 3ZYH 4A6S
• Related PRD ID: PRD_900037
• Descriptor: PA-I GALACTOPHILIC LECTIN, alpha-D-galactopyranose-(1-6)-alpha-D-glucopyranose, CALCIUM ION, ... (6 entities in total)
• Functional Keywords: sugar binding protein, galactose binding protein
• Biological source: PSEUDOMONAS AERUGINOSA
• Cellular location: Cytoplasm: Q05097
• Total number of polymer chains: 8
• Total formula weight: 104557.59

Authors

Blanchard, B.,Imberty, A.,Varrot, A. (deposition date: 2012-03-02, release date: 2013-03-20, Last modification date: 2023-12-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.75 Å)