1KUJ

Crystal structure of Jacalin complexed with 1-O-methyl-alpha-D-mannose

Summary for 1KUJ

• Entry DOI: 10.2210/pdb1kuj/pdb
• Related: 1jac 1jot 1ku8
• Descriptor: JACALIN ALPHA CHAIN, JACALIN BETA CHAIN, methyl alpha-D-mannopyranoside, ... (4 entities in total)
• Functional Keywords: lectin, beta-prism fold, carbohydrate binding, sugar binding protein
• Biological source: Artocarpus integer; More
• Total number of polymer chains: 8
• Total formula weight: 66958.90

Authors

Bourne, Y.,Astoul, C.H.,Zamboni, V.,Peumans, W.J.,Menu-Bouaouiche, L.,Van Damme, E.J.M.,Barre, A.,Rouge, P. (deposition date: 2002-01-22, release date: 2002-06-19, Last modification date: 2023-08-16)

Primary citation

Bourne, Y.,Astoul, C.H.,Zamboni, V.,Peumans, W.J.,Menu-Bouaouiche, L.,Van Damme, E.J.,Barre, A.,Rouge, P.
Structural basis for the unusual carbohydrate-binding specificity of jacalin towards galactose and mannose.
Biochem.J., 364:173-180, 2002

PubMed Abstract: Evidence is presented that the specificity of jacalin, the seed lectin from jack fruit (Artocarpus integrifolia), is not directed exclusively against the T-antigen disaccharide Galbeta1,3GalNAc, lactose and galactose, but also against mannose and oligomannosides. Biochemical analyses based on surface-plasmon-resonance measurements, combined with the X-ray-crystallographic determination of the structure of a jacalin-alpha-methyl-mannose complex at 2 A resolution, demonstrated clearly that jacalin is fully capable of binding mannose. Besides mannose, jacalin also interacts readily with glucose, N-acetylneuraminic acid and N-acetylmuramic acid. Structural analyses demonstrated that the relatively large size of the carbohydrate-binding site enables jacalin to accommodate monosaccharides with different hydroxyl conformations and provided unambiguous evidence that the beta-prism structure of jacalin is a sufficiently flexible structural scaffold to confer different carbohydrate-binding specificities to a single lectin.

PubMed: 11988090

Experimental method

X-RAY DIFFRACTION (2 Å)