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PDBsum entry 2x2s
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Cell adhesion
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PDB id
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2x2s
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the galnac/gal-Specific agglutinin from the phytopathogenic ascomycete sclerotinia sclerotiorum reveals novel adaptation of a beta-Trefoil domain.
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Authors
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G.Sulzenbacher,
V.Roig-Zamboni,
W.J.Peumans,
P.Rougé,
E.J.Van damme,
Y.Bourne.
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Ref.
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J Mol Biol, 2010,
400,
715-723.
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PubMed id
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Abstract
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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.
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