1ZLD
Crystal structure of a RGD-containing host-selective toxin: Pyrenophora tritici-repentis Ptr ToxA
1ZLD の概要
| エントリーDOI | 10.2210/pdb1zld/pdb |
| 関連するPDBエントリー | 1ZLE |
| 分子名称 | Ptr necrosis toxin, SULFATE ION (3 entities in total) |
| 機能のキーワード | beta-sandwich; rgd-motif, toxin |
| 由来する生物種 | Pyrenophora tritici-repentis |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 13399.88 |
| 構造登録者 | Sarma, G.N.,Manning, V.A.,Ciuffetti, L.M.,Karplus, P.A. (登録日: 2005-05-06, 公開日: 2005-08-16, 最終更新日: 2024-11-06) |
| 主引用文献 | Sarma, G.N.,Manning, V.A.,Ciuffetti, L.M.,Karplus, P.A. Structure of Ptr ToxA: An RGD-Containing Host-Selective Toxin from Pyrenophora tritici-repentis Plant Cell, 17:3190-3202, 2005 Cited by PubMed Abstract: 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. PubMed: 16214901DOI: 10.1105/tpc.105.034918 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.65 Å) |
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