5MIH

Crystal structure of the lectin LecA from Pseudomonas aeruginosa in complex with a phenyl-epoxy-galactopyranoside

Summary for 5MIH

• Entry DOI: 10.2210/pdb5mih/pdb
• Descriptor: PA-I galactophilic lectin, CALCIUM ION, phenyl 6,7-anhydro-D-glycero-beta-D-galacto-heptopyranoside, ... (5 entities in total)
• Functional Keywords: lectin, galactose binding protein, covalent lectin inhibition, sugar binding protein
• Biological source: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
• Cellular location: Cytoplasm: Q05097
• Total number of polymer chains: 4
• Total formula weight: 52522.16

Authors

Wagner, S.,Hauk, D.,Hofmann, M.,Joachim, I.,Sommer, R.,Muller, R.,Imberty, A.,Varrot, A.,Titz, A. (deposition date: 2016-11-28, release date: 2017-10-11, Last modification date: 2024-01-17)

Primary citation

Wagner, S.,Hauck, D.,Hoffmann, M.,Sommer, R.,Joachim, I.,Muller, R.,Imberty, A.,Varrot, A.,Titz, A.
Covalent Lectin Inhibition and Application in Bacterial Biofilm Imaging.
Angew. Chem. Int. Ed. Engl., 56:16559-16564, 2017

PubMed Abstract: Biofilm formation by pathogenic bacteria is a hallmark of chronic infections. In many cases, lectins play key roles in establishing biofilms. The pathogen Pseudomonas aeruginosa often exhibiting various drug resistances employs its lectins LecA and LecB as virulence factors and biofilm building blocks. Therefore, inhibition of the function of these proteins is thought to have potential in developing "pathoblockers" preventing biofilm formation and virulence. A covalent lectin inhibitor specific to a carbohydrate binding site is described for the first time. Its application in the LecA-specific in vitro imaging of biofilms formed by P. aeruginosa is also reported.

PubMed: 28960731
DOI: 10.1002/anie.201709368

Experimental method

X-RAY DIFFRACTION (1.8 Å)