Download MendeleyThe 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, W.J., Astoul, C.H., Van Damme, E.J.M., Rouge, P.(2004) J Biol Chem 279: 527-533
- PubMed: 14561768
- DOI: https://doi.org/10.1074/jbc.M308218200
- Primary Citation of Related Structures:
1OUW - PubMed Abstract:
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.
Organizational Affiliation:
AFMB-CNRS, CNRS UMR6098, F13402 Marseille Cedex 20, France. [email protected]
