4AL9: Crystal Structure Of The Lectin Pa-il From Pseudomonas Aeruginoas In Complex With Melibiose

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 alpha-galactoside residues and displays strong affinity for melibiose (alphaGal1-6Glc) with a Kd of 38.8 microM. The crystal structure of LecA/melibiose complex shows classical calcium-bridged binding of alphaGal 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.
PDB ID: 4AL9Download
MMDB ID: 108392
PDB Deposition Date: 2012/3/2
Updated in MMDB: 2013/10
Experimental Method:
x-ray diffraction
Resolution: 1.75  Å
Source Organism:
Similar Structures:
Biological Unit for 4AL9: tetrameric; determined by author and by software (PISA)
Molecular Components in 4AL9
Label Count Molecule
Proteins (4 molecules)
Pa-i Galactophilic Lectin(Gene symbol: lecA)
Molecule annotation
Chemicals (10 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB