1zld: Difference between revisions

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[[Image:1zld.gif|left|200px]]
{{Seed}}
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{{STRUCTURE_1zld|  PDB=1zld  |  SCENE=  }}  
{{STRUCTURE_1zld|  PDB=1zld  |  SCENE=  }}  


'''Crystal structure of a RGD-containing host-selective toxin: Pyrenophora tritici-repentis Ptr ToxA'''
===Crystal structure of a RGD-containing host-selective toxin: Pyrenophora tritici-repentis Ptr ToxA===




==Overview==
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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, beta-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.
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{{ABSTRACT_PUBMED_16214901}}


==About this Structure==
==About this Structure==
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[[Category: Beta-sandwich]]
[[Category: Beta-sandwich]]
[[Category: Rgd-motif]]
[[Category: Rgd-motif]]
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