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|  | ==Solution structure of M. oryzae protein AVR1-CO39== |  | ==Solution structure of M. oryzae protein AVR1-CO39== | 
| - | <StructureSection load='2myv' size='340' side='right' caption='[[2myv]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2myv' size='340' side='right'caption='[[2myv]]' scene=''> | 
|  | == Structural highlights == |  | == Structural highlights == | 
| - | <table><tr><td colspan='2'>[[2myv]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MYV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MYV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2myv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyricularia_grisea Pyricularia grisea]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MYV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MYV FirstGlance]. <br> | 
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2myw|2myw]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr> | 
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2myv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2myv OCA], [http://pdbe.org/2myv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2myv RCSB], [http://www.ebi.ac.uk/pdbsum/2myv PDBsum]</span></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=2myv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2myv OCA], [https://pdbe.org/2myv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2myv RCSB], [https://www.ebi.ac.uk/pdbsum/2myv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2myv ProSAT]</span></td></tr> | 
|  | </table> |  | </table> | 
|  | + | == Function == | 
|  | + | [https://www.uniprot.org/uniprot/Q8J180_PYRGI Q8J180_PYRGI]  | 
|  | <div style="background-color:#fffaf0;"> |  | <div style="background-color:#fffaf0;"> | 
|  | == Publication Abstract from PubMed == |  | == Publication Abstract from PubMed == | 
| Line 19: | Line 22: | 
|  | __TOC__ |  | __TOC__ | 
|  | </StructureSection> |  | </StructureSection> | 
| - | [[Category: Guillen, K de]] | + | [[Category: Large Structures]] | 
| - | [[Category: Kroj, T]] | + | [[Category: Pyricularia grisea]] | 
| - | [[Category: Unknown function]] | + | [[Category: Kroj T]] | 
|  | + | [[Category: De Guillen K]] | 
|  |   Structural highlights   Function Q8J180_PYRGI 
 
  Publication Abstract from PubMed Phytopathogenic ascomycete fungi possess huge effector repertoires that are dominated by hundreds of sequence-unrelated small secreted proteins. The molecular function of these effectors and the evolutionary mechanisms that generate this tremendous number of singleton genes are largely unknown. To get a deeper understanding of fungal effectors, we determined by NMR spectroscopy the 3-dimensional structures of the Magnaporthe oryzae effectors AVR1-CO39 and AVR-Pia. Despite a lack of sequence similarity, both proteins have very similar 6 beta-sandwich structures that are stabilized in both cases by a disulfide bridge between 2 conserved cysteins located in similar positions of the proteins. Structural similarity searches revealed that AvrPiz-t, another effector from M. oryzae, and ToxB, an effector of the wheat tan spot pathogen Pyrenophora tritici-repentis have the same structures suggesting the existence of a family of sequence-unrelated but structurally conserved fungal effectors that we named MAX-effectors (Magnaporthe Avrs and ToxB like). Structure-informed pattern searches strengthened this hypothesis by identifying MAX-effector candidates in a broad range of ascomycete phytopathogens. Strong expansion of the MAX-effector family was detected in M. oryzae and M. grisea where they seem to be particularly important since they account for 5-10% of the effector repertoire and 50% of the cloned avirulence effectors. Expression analysis indicated that the majority of M. oryzae MAX-effectors are expressed specifically during early infection suggesting important functions during biotrophic host colonization. We hypothesize that the scenario observed for MAX-effectors can serve as a paradigm for ascomycete effector diversity and that the enormous number of sequence-unrelated ascomycete effectors may in fact belong to a restricted set of structurally conserved effector families.
 Structure Analysis Uncovers a Highly Diverse but Structurally Conserved Effector Family in Phytopathogenic Fungi.,de Guillen K, Ortiz-Vallejo D, Gracy J, Fournier E, Kroj T, Padilla A PLoS Pathog. 2015 Oct 27;11(10):e1005228. doi: 10.1371/journal.ppat.1005228., eCollection 2015 Oct. PMID:26506000[1]
 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
   References ↑ de Guillen K, Ortiz-Vallejo D, Gracy J, Fournier E, Kroj T, Padilla A. Structure Analysis Uncovers a Highly Diverse but Structurally Conserved Effector  Family in Phytopathogenic Fungi. PLoS Pathog. 2015 Oct 27;11(10):e1005228. doi: 10.1371/journal.ppat.1005228., eCollection 2015 Oct. PMID:26506000 doi:http://dx.doi.org/10.1371/journal.ppat.1005228
 
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