4LK6

Crystal Structure of Pseudomonas aeruginosa Lectin LecA Complexed with Chlorophenol Red-b-D-galactopyranoside at 2.86 A Resolution

Summary for 4LK6

• Entry DOI: 10.2210/pdb4lk6/pdb
• Related: 4LJH 4LK7
• Descriptor: PA-I galactophilic lectin, CALCIUM ION, 2-[(E)-(3-chloro-4-hydroxyphenyl)(3-chloro-4-oxocyclohexa-2,5-dien-1-ylidene)methyl]benzenesulfonic acid, ... (5 entities in total)
• Functional Keywords: lectin fold, sugar binding protein, galactose
• Biological source: Pseudomonas aeruginosa
• Cellular location: Cytoplasm: Q05097
• Total number of polymer chains: 12
• Total formula weight: 160963.66

Authors

Kadam, R.U.,Stocker, A.,Reymond, J.L. (deposition date: 2013-07-06, release date: 2013-10-30, Last modification date: 2023-11-08)

Primary citation

Kadam, R.U.,Garg, D.,Schwartz, J.,Visini, R.,Sattler, M.,Stocker, A.,Darbre, T.,Reymond, J.L.
CH-pi "T-Shape" Interaction with Histidine Explains Binding of Aromatic Galactosides to Pseudomonas aeruginosa Lectin LecA
Acs Chem.Biol., 8:1925-1930, 2013

PubMed Abstract: The galactose specific lectin LecA mediates biofilm formation in the opportunistic pathogen P. aeruginosa . The interaction between LecA and aromatic β-galactoside biofilm inhibitors involves an intermolecular CH-π T-shape interaction between C(ε1)-H of residue His50 in LecA and the aromatic ring of the galactoside aglycone. The generality of this interaction was tested in a diverse family of β-galactosides. LecA binding to aromatic β-galactosides (KD ∼ 8 μM) was consistently stronger than to aliphatic β-galactosides (KD ∼ 36 μM). The CH-π interaction was observed in the X-ray crystal structures of six different LecA complexes, with shorter than the van der Waals distances indicating productive binding. Related XH/cation/π-π interactions involving other residues were identified in complexes of aromatic glycosides with a variety of carbohydrate binding proteins such as concanavalin A. Exploiting such interactions might be generally useful in drug design against these targets.

PubMed: 23869965
DOI: 10.1021/cb400303w

Experimental method

X-RAY DIFFRACTION (2.859 Å)