Structure of Ptr ToxA: An RGD-containing host-selective toxin from Pyrenophora tritici-repentis
Plant Cell, ISSN: 1040-4651, Vol: 17, Issue: 11, Page: 3190-3202
2005
- 100Citations
- 86Captures
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Metrics Details
- Citations100
- Citation Indexes100
- 100
- CrossRef79
- Captures86
- Readers86
- 86
Article Description
Tan spot of wheat (Triticum aestivum), caused by the fungus Pyrenophora tritici-repentis, has significant agricultural and economic impact. Ptr ToxA (ToxA), the first discovered proteinaceous host-selective toxin, is produced by certain P. tritici-repentis races and is necessary and sufficient to cause cell death in sensitive wheat cultivars. We present here the high-resolution crystal structure of ToxA in two different crystal forms, providing four independent views of the protein. ToxA adopts a single-domain, β-sandwich fold of novel topology. Mapping of the existing mutation data onto the structure supports the hypothesized importance of an Arg-Gly-Asp (RGD) and surrounding sequence. Its occurrence in a single, solvent-exposed loop in the protein suggests that it is directly involved in recognition events required for ToxA action. Furthermore, the ToxA structure reveals a surprising similarity with the classic mammalian RGD-containing domain, the fibronectin type III (FnIII) domain: the two topologies are related by circular permutation. The similar topologies and the positional conservation of the RGD-containing loop raises the possibility that ToxA is distantly related to mammalian FnIII proteins and that to gain entry it binds to an integrin-like receptor in the plant host. © 2005 American Society of Plant Biologists.
Bibliographic Details
Oxford University Press (OUP)
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