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Secondary sugar binding site identified for LecA lectin from Pseudomonas aeruginosa
Author(s) -
Blanchard Bertrand,
Imberty Anne,
Varrot Annabelle
Publication year - 2014
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.24430
Subject(s) - lectin , melibiose , binding site , pseudomonas aeruginosa , biochemistry , biofilm , galactose , chemistry , sugar , microbiology and biotechnology , mannan binding lectin , c type lectin , bacteria , biology , sucrose , genetics , maltose
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 K d of 38.8 µ M . 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. Proteins 2014; 82:1060–1065. © 2013 Wiley Periodicals, Inc.