PDBsum entry: 2i0w

Antifungal protein

PDB-id: 2i0w

Contents

Description

Header details

Header records

References

PROCHECK

Protein chain

207 a.a. *

Metal ions

_CL

Waters ×67

* Residue conservation analysis

Tools

Clefts Calculation

PDB id:

2i0w

Name:

Antifungal protein

Title:

Crystal structure analysis of np24-i, a thaumatin-like protein

Structure:

Protein np24. Chain: a. Synonym: pathogenesis-related protein pr p23, salt-induced protein

Source:

Solanum lycopersicum. Organism_taxid: 4081. Other_details: ripe tomato

UniProt:

P12670 (NP24_SOLLC)

Seq:

247 a.a.

Struc:

207 a.a.

Key:	PfamA domain
Secondary structure	CATH domain

Resolution:

2.50Å

R-factor:

0.171

R-free:

0.223

Authors:

C.Chakrabarti,R.Ghosh

Key ref:

R.Ghosh and C.Chakrabarti (2008). Crystal structure analysis of NP24-I: a thaumatin-like protein.. Planta, 228, 883-890. [PubMed id: 18651170] [DOI: 10.1007/s00425-008-0790-5]

Date:

11-Aug-06

Release date:

24-Jul-07

Quick_links

Procheck

Clefts

Surface

Key reference

DOI no: 10.1007/s00425-008-0790-5

Planta 228:883-890 (2008)

PubMed id: 18651170

Crystal structure analysis of NP24-I: a thaumatin-like protein.

R.Ghosh, C.Chakrabarti.

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.