1ouw

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spinqualitylabelsall models 1ouw, resolution 1.37Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of Calystegia sepium agglutinin

Overview

The high number of quaternary structures observed for lectins highlights, the important role of these oligomeric assemblies during carbohydrate, recognition events. Although a large diversity in the mode of association, of lectin subunits is frequently observed, the oligomeric assemblies of, plant lectins display small variations within a single family. The crystal, structure of the mannose-binding jacalin-related lectin from Calystegia, sepium (Calsepa) has been determined at 1.37-A resolution. Calsepa, exhibits the same beta-prism fold as identified previously for other, members of the family, but the shape and the hydrophobic character of its, carbohydrate-binding site is unlike that of other members, consistent with, surface plasmon resonance analysis showing a preference for methylated, sugars. Calsepa reveals a novel dimeric assembly markedly dissimilar to, those described earlier for Heltuba and jacalin but mimics the canonical, 12-stranded beta-sandwich dimer found in legume lectins. The present, structure exemplifies the adaptability of the beta-prism building block in, the evolution of plant lectins and highlights the biological role of these, quaternary structures for carbohydrate recognition.

About this Structure

1OUW is a Single protein structure of sequence from Calystegia sepium with MLT, EDO and IMD as ligands. Full crystallographic information is available from OCA.

Reference

The crystal structure of the Calystegia sepium agglutinin reveals a novel quaternary arrangement of lectin subunits with a beta-prism fold., Bourne Y, Roig-Zamboni V, Barre A, Peumans WJ, Astoul CH, Van Damme EJ, Rouge P, J Biol Chem. 2004 Jan 2;279(1):527-33. Epub 2003 Oct 15. PMID:14561768

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