2I0W

Crystal structure analysis of NP24-I, a thaumatin-like protein

Summary for 2I0W

• Entry DOI: 10.2210/pdb2i0w/pdb
• Descriptor: Protein NP24, CHLORIDE ION (3 entities in total)
• Functional Keywords: alpha-beta protein, antifungal protein
• Biological source: Solanum lycopersicum
• Cellular location: Cytoplasm: P12670
• Total number of polymer chains: 1
• Total formula weight: 22267.52

Authors

Chakrabarti, C.,Ghosh, R. (deposition date: 2006-08-11, release date: 2007-07-24, Last modification date: 2024-10-30)

Primary citation

Ghosh, R.,Chakrabarti, C.
Crystal structure analysis of NP24-I: a thaumatin-like protein
Planta, 228:883-890, 2008

PubMed 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.

PubMed: 18651170
DOI: 10.1007/s00425-008-0790-5

Experimental method

X-RAY DIFFRACTION (2.5 Å)