Εξειδίκευση τύπου :	Άρθρο σε επιστημονικό περιοδικό
Τίτλος:	Structural analysis of the Rhizoctonia solani agglutinin reveals a domain-swapping dimeric assembly
Δημιουργός/Συγγραφέας:	Skamnaki V.T. Peumans W.J. Kantsadi A.L. Cubeta M.A. Plas K. Pakala S. [EL] Ζωγράφος, Σπύρος Ε.[EN] Zographos, Spyros E. Smagghe G. Nierman W.C. Van Damme E.J.M. [EL] Λεωνίδας, Δημήτρης Δ.[EN] Leonidas, Demetres D.
Ημερομηνία:	2013
Γλώσσα:	Αγγλικά
ISSN:	1742-464X
DOI:	10.1111/febs.12190
Άλλο:	PubMed ID: 23402398
Περίληψη:	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) The amino acid sequence and the crystal structures of the free form and in complex with GalNAc of Rhizoctonia solani agglutinin (RSA), a 15.5 kDa lectin accumulated in the mycelium and sclerotia of the soil born plant pathogenic fungus R. solani are presented. Each monomer accommodates two carbohydrate binding sites while their assembly involves an N-terminal swap, novel to R-type lectins.
Τίτλος πηγής δημοσίευσης:	FEBS Journal
Τόμος/Κεφάλαιο:	280
Τεύχος:	8
Σελίδες:	1750-1763
Θεματική Κατηγορία:	[EL] Βιολογία (Γενικά)[EN] Biology (General) [EL] Χημεία (Γενικά)[EN] Chemistry (General)
Λέξεις-Κλειδιά:	β-trefoil domain crystallography fungal lectin galactose glycan array
Αξιολόγηση από ομότιμους (peer reviewed):	Ναι
Κάτοχος πνευματικών δικαιωμάτων:	© 2013 The Authors Journal compilation © 2013 FEBS.
Όροι και προϋποθέσεις δικαιωμάτων:	All Open Access, Bronze
Εμφανίζεται στις συλλογές:	Ινστιτούτο Χημικής Βιολογίας - Επιστημονικό έργο