1zle: Difference between revisions

Revision as of 17:16, 21 February 2008

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

OverviewOverview

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.

About this StructureAbout this Structure

1ZLE is a Single protein structure of sequence from Pyrenophora tritici-repentis with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Structure of Ptr ToxA: an RGD-containing host-selective toxin from Pyrenophora tritici-repentis., Sarma GN, Manning VA, Ciuffetti LM, Karplus PA, Plant Cell. 2005 Nov;17(11):3190-202. Epub 2005 Oct 7. PMID:16214901

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 ==Overview==
-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.
+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.
 ==About this Structure==
@@ Line 13: / Line 13: @@
 [[Category: Pyrenophora tritici-repentis]]
 [[Category: Single protein]]
-[[Category: Ciuffetti, L.M.]]
+[[Category: Ciuffetti, L M.]]
-[[Category: Karplus, P.A.]]
+[[Category: Karplus, P A.]]
-[[Category: Manning, V.A.]]
+[[Category: Manning, V A.]]
-[[Category: Sarma, G.N.]]
+[[Category: Sarma, G N.]]
 [[Category: NI]]
 [[Category: beta-sandwich; rgd-motif]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 17:37:26 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:16:53 2008''