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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
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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

Sarma, Ganapathy N.; Manning, Viola A.; Ciuffetti, Lynda M.; Karplus, P. Andrew

Oxford University Press (OUP)

Agricultural and Biological Sciences; Biochemistry, Genetics and Molecular Biology

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