title: Crystal structure analysis of NP24-I: a thaumatin-like protein.
abstract: The crystal structure of NP24-I, an isoform of the thaumatin-like protein (TLP) NP24 from tomato, has been reported. A prominent acidic cleft is observed between domains I and II of the three-domain structure of this antifungal protein, a feature common to other antifungal TLPs. The defensive role of the TLPs has also been attributed to their beta-1,3-glucanase activity and here too the acidic cleft is reported to play a vital role. NP24 is known to bind beta-glucans and so a linear beta-1,3-glucan molecule has been docked in the interdomain cleft of NP24-I. From the docked complex it is observed that the beta-glucan chain is so positioned in the cleft that a Glu and Asp residue on either side of it may form a catalytic pair to cause the cleavage of a glycosidic bond. NP24 has been reported to be an allergenic protein and an allergenic motif could be identified on the surface of the helical domain II of NP24-I. In addition, some allergenic motifs bearing high similarity/identity with some predicted Ig-E binding motifs of closely related allergenic TLPs like Jun a 3 (Juniperus ashei, from mountain cedar pollen) and banana-TLP have been identified on the molecular surface of NP24-I.
authors.affiliation: Crystallography and Molecular Biology Division, Saha Institute of Nuclear Physics, 1/AF Bidhannagar, Kolkata 700 064, India.
authors.forename: Raka
authors.initials: R
authors.lastname: Ghosh
authors.forename: Chandana
authors.initials: C
authors.lastname: Chakrabarti
mesh_terms: D000935:Antifungal Agents / Q000737:chemistry / Q000378:metabolism; D018360:Crystallography, X-Ray / Q000379:methods; D018551:Solanum lycopersicum / Q000235:genetics / Q000378:metabolism*; D010940:Plant Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
chemical_list: D000935:Antifungal Agents; D010940:Plant Proteins; C003427:thaumatin protein, plant