4G9M

Crystal structure of the Rhizoctonia solani agglutinin

4G9M の概要

• エントリーDOI: 10.2210/pdb4g9m/pdb
• 関連するPDBエントリー: 4G9N
• 分子名称: agglutinin (2 entities in total)
• 機能のキーワード: lectin, carbohydrate-binding specificity, sugar binding protein
• 由来する生物種: Rhizoctonia solani
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 30966.31

構造登録者

Skamnaki, V.T.,Kantsadi, A.L.,Leonidas, D.D. (登録日: 2012-07-24, 公開日: 2013-06-05, 最終更新日: 2023-09-13)

主引用文献

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

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: 23402398
DOI: 10.1111/febs.12190

実験手法

X-RAY DIFFRACTION (1.601 Å)