PDBsum entry 2x2s

Cell adhesion

PDB id: 2x2s

Contents

Protein chains

150 a.a. *

Ligands

GOL ×2

Waters ×710

* Residue conservation analysis

PDB id:

2x2s

Name:

Cell adhesion

Title:

Crystal structure of sclerotinia sclerotiorum agglutinin ssa

Structure:

Agglutinin. Chain: a, b, c, d. Synonym: agglutinin ssa

Source:

Sclerotinia sclerotiorum. Organism_taxid: 5180

Resolution:

1.60Å R-factor: 0.141 R-free: 0.162

Authors:

G.Sulzenbacher,V.Roig-Zamboni,W.J.Peumans,P.Rouge,E.J.M.Van Damme, Y.Bourne

Key ref:

G.Sulzenbacher et al. (2010). 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, 715-723. PubMed id: 20566411

Date:

15-Jan-10 Release date: 26-May-10

Protein chains

A7XUK7  (AGGL_SCLSC) -  Agglutinin from Sclerotinia sclerotiorum

Seq: 153 a.a.

Struc: 150 a.a.

Enzyme reactions

• Enzyme class: E.C.?

J Mol Biol 400:715-723 (2010)

PubMed id: 20566411

Crystal structure of the GalNAc/Gal-specific agglutinin from the phytopathogenic ascomycete Sclerotinia sclerotiorum reveals novel adaptation of a beta-trefoil domain.

G.Sulzenbacher, V.Roig-Zamboni, W.J.Peumans, P.Rougé, E.J.Van Damme, Y.Bourne.

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.