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protein metals links
Antifungal protein PDB id
2i0w
Jmol
Contents
Protein chain
207 a.a. *
Metals
_CL
Waters ×67
* Residue conservation analysis
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
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    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P12670  (NP24_SOLLC) -  Protein NP24
Seq:
Struc: 		247 a.a.
207 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     response to stress   5 terms 

 

 
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.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21324123 B.Petre, I.Major, N.Rouhier, and S.Duplessis (2011).
Genome-wide analysis of eukaryote thaumatin-like proteins (TLPs) with an emphasis on poplar.
  BMC Plant Biol, 11, 33.  
19997927 J.J.Liu, A.Zamani, and A.K.Ekramoddoullah (2010).
Expression profiling of a complex thaumatin-like protein family in western white pine.
  Planta, 231, 637-651.  
20204373 J.J.Liu, R.Sturrock, and A.K.Ekramoddoullah (2010).
The superfamily of thaumatin-like proteins: its origin, evolution, and expression towards biological function.
  Plant Cell Rep, 29, 419-436.  
20645107 J.P.Zhao, and X.H.Su (2010).
Patterns of molecular evolution and predicted function in thaumatin-like proteins of Populus trichocarpa.
  Planta, 232, 949-962.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.