4G9M
Crystal structure of the Rhizoctonia solani agglutinin
Summary for 4G9M
| Entry DOI | 10.2210/pdb4g9m/pdb |
| Related | 4G9N |
| Descriptor | agglutinin (2 entities in total) |
| Functional Keywords | lectin, carbohydrate-binding specificity, sugar binding protein |
| Biological source | Rhizoctonia solani |
| Total number of polymer chains | 2 |
| Total formula weight | 30966.31 |
| Authors | Skamnaki, V.T.,Kantsadi, A.L.,Leonidas, D.D. (deposition date: 2012-07-24, release date: 2013-06-05, Last modification date: 2023-09-13) |
| Primary citation | Skamnaki, V.T.,Peumans, W.J.,Kantsadi, A.L.,Cubeta, M.A.,Plas, K.,Pakala, S.,Zographos, S.E.,Smagghe, G.,Nierman, W.C.,Van Damme, E.J.,Leonidas, D.D. Structural analysis of the Rhizoctonia solani agglutinin reveals a domain-swapping dimeric assembly. Febs J., 280:1750-1763, 2013 Cited by PubMed Abstract: Rhizoctonia solani agglutinin (RSA) is a 15.5-kDa lectin accumulated in the mycelium and sclerotia of the soil born plant pathogenic fungus R. solani. Although it is considered to serve as a storage protein and is implicated in fungal insecticidal activity, its physiological role remains unclear as a result of a lack of any structure/function relationship information. Glycan arrays showed that RSA displays high selectivity towards terminal nonreducing N-acetylgalactosamine residues. We determined the amino acid sequence of RSA and also determined the crystal structures of the free form and the RSA-N-acetylgalactosamine complex at 1.6 and 2.2 Å resolution, respectively. RSA is a homodimer comprised of two monomers adopting the β-trefoil fold. Each monomer accommodates two different carbohydrate-binding sites in an asymmetric way. Despite RSA topology similarities with R-type lectins, the two-monomer assembly involves an N-terminal swap, thus creating a dimer association novel to R-type lectins. Structural characterization of the two carbohydrate-binding sites offers insights on the structural determinants of the RSA carbohydrate specificity. PubMed: 23402398DOI: 10.1111/febs.12190 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.601 Å) |
Structure validation
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