4g9n

Publication Abstract from PubMed

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 A resolution, respectively. RSA is a homodimer comprised of two monomers adopting the beta-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. DATABASE: Structural data have been deposited in the Protein Data Bank database under accession numbers 4G9M and 4G9N. STRUCTURED DIGITAL ABSTRACT: RSA and RSA bind by x-ray crystallography (View interaction).

Structural analysis of the Rhizoctonia solani agglutinin reveals a domain-swapping dimeric assembly.,Skamnaki VT, Peumans WJ, Kantsadi AL, Cubeta MA, Plas K, Pakala S, Zographos SE, Smagghe G, Nierman WC, Van Damme EJ, Leonidas DD FEBS J. 2013 Apr;280(8):1750-63. doi: 10.1111/febs.12190. Epub 2013 Mar 7. PMID:23402398^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.