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FEBS J. 2013 Apr;280(8):1750-63. doi: 10.1111/febs.12190. Epub 2013 Mar 7.

Structural analysis of the Rhizoctonia solani agglutinin reveals a domain-swapping dimeric assembly.

Author information

1
Department of Biochemistry and Biotechnology, University of Thessaly, Larissa, Greece.

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.

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).

PMID:
23402398
DOI:
10.1111/febs.12190
[Indexed for MEDLINE]
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