2BIC

The solution structure of the recombinant elicitor protein PcF from the oomycete pathogen P. cactorum

Summary for 2BIC

• Entry DOI: 10.2210/pdb2bic/pdb
• NMR Information: BMRB: 6520
• Descriptor: PHYTOTOXIC PROTEIN PCF (1 entity in total)
• Functional Keywords: plant pathogen, phytophthora cactorum fragaria protein, oomycete plant pathogen, elicitin family, toxin
• Biological source: PHYTOPHTHORA CACTORUM
• Total number of polymer chains: 1
• Total formula weight: 5617.18

Authors

Nicastro, G.,Orsomando, G.,Desario, F.,Ferrari, E.,Manconi, L.,Spisni, A.,Ruggieri, S. (deposition date: 2005-01-20, release date: 2006-06-28, Last modification date: 2024-10-09)

Primary citation

Nicastro, G.,Orsomando, G.,Ferrari, E.,Manconi, L.,Desario, F.,Amici, A.,Naso, A.,Carpaneto, A.,Pertinhez, T.A.,Ruggieri, S.,Spisni, A.
Solution Structure of the Phytotoxic Protein Pcf: The First Characterized Member of the Phytophthora Pcf Toxin Family.
Protein Sci., 18:1786-, 2009

PubMed Abstract: The PcF protein from Phytophthora cactorum is the first member of the "PcF toxin family" from the plant pathogens Phytophthora spp. It is able to induce withering in tomato and strawberry leaves. The lack of sequence similarity with other proteins hampers the identification of the molecular mechanisms responsible for its toxicity. Here, we show that the six cysteines form a disulphide pattern that is exclusive for PcF and essential for the protein withering activity. The NMR solution structure identifies a novel fold among protein effectors: a helix-loop-helix motif. The presence of a negatively charged surface suggests that it might act as a site of electrostatic interaction. Interestingly, a good fold match with Ole e 6, a plant protein with allergenic activity, highlighted the spatial superimposition of a stretch of identical residues. This finding suggests a possible biological activity based on molecular mimicry.

PubMed: 19554629
DOI: 10.1002/PRO.168

Experimental method

SOLUTION NMR