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< | ==Crystal structure of a RGD-containing host-selective toxin: Pyrenophora tritici-repentis Ptr ToxA== | ||
<StructureSection load='1zle' size='340' side='right'caption='[[1zle]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1zle]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrenophora_tritici-repentis Pyrenophora tritici-repentis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZLE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZLE FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | |||
--> | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zle FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zle OCA], [https://pdbe.org/1zle PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zle RCSB], [https://www.ebi.ac.uk/pdbsum/1zle PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zle ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/P78737_9PLEO P78737_9PLEO] | |||
<div style="background-color:#fffaf0;"> | |||
== | == Publication Abstract from PubMed == | ||
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. | ||
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<ref>PMID:16214901</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1zle" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pyrenophora tritici-repentis]] | [[Category: Pyrenophora tritici-repentis]] | ||
[[Category: Ciuffetti LM]] | |||
[[Category: Ciuffetti | [[Category: Karplus PA]] | ||
[[Category: Karplus | [[Category: Manning VA]] | ||
[[Category: Manning | [[Category: Sarma GN]] | ||
[[Category: Sarma | |||
Latest revision as of 10:53, 12 July 2023
Crystal structure of a RGD-containing host-selective toxin: Pyrenophora tritici-repentis Ptr ToxACrystal structure of a RGD-containing host-selective toxin: Pyrenophora tritici-repentis Ptr ToxA
Structural highlights
FunctionPublication Abstract from PubMedTan 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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