4al9
From Proteopedia
Crystal structure of the lectin PA-IL from Pseudomonas aeruginoas in complex with melibiose
Structural highlights
FunctionPA1L_PSEAE D-galactose specific lectin. Binds in decreasing order of affinity: melibiose, methyl-alpha-D-galactoside, D-galactose, methyl-beta-D-galactoside, N-acetyl-D-galactosamine. Similar to plant lectins in its selective (carbohydrate-specific) hemagglutinating activity. Publication Abstract from PubMedThe 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. Secondary sugar binding site identified for LecA lectin from Pseudomonas aeruginosa.,Blanchard B, Imberty A, Varrot A Proteins. 2013 Oct 1. doi: 10.1002/prot.24430. PMID:24123124[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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