2X2S

Crystal structure of Sclerotinia sclerotiorum agglutinin SSA

Summary for 2X2S

• Entry DOI: 10.2210/pdb2x2s/pdb
• Related: 2X2T
• Descriptor: AGGLUTININ, GLYCEROL (3 entities in total)
• Functional Keywords: fungal lectin, beta-trefoil domain, cell adhesion
• Biological source: SCLEROTINIA SCLEROTIORUM
• Total number of polymer chains: 4
• Total formula weight: 67214.59

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: 2024-05-01)

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

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: 20566411
DOI: 10.1016/J.JMB.2010.05.038

Experimental method

X-RAY DIFFRACTION (1.6 Å)