1OUW
Crystal structure of Calystegia sepium agglutinin
Summary for 1OUW
| Entry DOI | 10.2210/pdb1ouw/pdb |
| Related | 1C3K 1C3M 1C3N |
| Descriptor | lectin, 1,2-ETHANEDIOL, IMIDAZOLE, ... (5 entities in total) |
| Functional Keywords | beta-prism fold, agglutinin, lectin, mannose-binding, jacalin-related, sugar binding protein |
| Biological source | Calystegia sepium (hedge bindweed) |
| Total number of polymer chains | 4 |
| Total formula weight | 65045.73 |
| Authors | Bourne, Y.,Roig-Zamboni, V.,Barre, A.,Peumans, W.J.,Astoul, C.H.,van Damme, E.J.M.,Rouge, P. (deposition date: 2003-03-25, release date: 2003-11-11, Last modification date: 2025-03-26) |
| Primary citation | Bourne, Y.,Roig-Zamboni, V.,Barre, A.,Peumans, W.J.,Astoul, C.H.,Van Damme, E.J.M.,Rouge, P. The crystal structure of the Calystegia sepium agglutinin reveals a novel quaternary arrangement of lectin subunits with a beta-prism fold J.Biol.Chem., 279:527-533, 2004 Cited by 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. PubMed: 14561768DOI: 10.1074/jbc.M308218200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.37 Å) |
Structure validation
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