2X2T
CRYSTAL STRUCTURE OF SCLEROTINIA SCLEROTIORUM AGGLUTININ SSA in complex with Gal-beta1,3-Galnac
Summary for 2X2T
| Entry DOI | 10.2210/pdb2x2t/pdb |
| Related | 2X2S |
| Descriptor | AGGLUTININ, beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | fungal lectin, beta-trefoil domain, cell adhesion |
| Biological source | SCLEROTINIA SCLEROTIORUM |
| Total number of polymer chains | 1 |
| Total formula weight | 17913.65 |
| Authors | Sulzenbacher, G.,Roig-Zamboni, V.,Peumans, W.J.,Rouge, P.,Van Damme, E.J.M.,Bourne, Y. (deposition date: 2010-01-15, release date: 2010-05-26, Last modification date: 2023-12-20) |
| Primary citation | Sulzenbacher, G.,Roig-Zamboni, V.,Peumans, W.J.,Rouge, P.,Van Damme, E.J.M.,Bourne, Y. Crystal Structure of the Galnac/Gal-Specific Agglutinin from the Phytopathogenic Ascomycete Sclerotinia Sclerotiorum Reveals Novel Adaptation of a Beta-Trefoil Domain J.Mol.Biol., 400:715-, 2010 Cited by PubMed Abstract: A lectin from the phytopathogenic ascomycete Sclerotinia sclerotiorum that shares only weak sequence similarity with characterized fungal lectins has recently been identified. S. sclerotiorum agglutinin (SSA) is a homodimeric protein consisting of two identical subunits of approximately 17 kDa and displays specificity primarily towards Gal/GalNAc. Glycan array screening indicates that SSA readily interacts with Gal/GalNAc-bearing glycan chains. The crystal structures of SSA in the ligand-free form and in complex with the Gal-beta1,3-GalNAc (T-antigen) disaccharide have been determined at 1.6 and 1.97 A resolution, respectively. SSA adopts a beta-trefoil domain as previously identified for other carbohydrate-binding proteins of the ricin B-like lectin superfamily and accommodates terminal non-reducing galactosyl and N-acetylgalactosaminyl glycans. Unlike other structurally related lectins, SSA contains a single carbohydrate-binding site at site alpha. SSA reveals a novel dimeric assembly markedly dissimilar to those described earlier for ricin-type lectins. The present structure exemplifies the adaptability of the beta-trefoil domain in the evolution of fungal lectins. PubMed: 20566411DOI: 10.1016/J.JMB.2010.05.038 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.97 Å) |
Structure validation
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