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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 with sequence from [https://en.wikipedia.org/wiki/Cbs_138707_[[pyricularia_grisea]] Cbs 138707 [[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> | + | <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"><div style='overflow: auto; max-height: 3em;'>[[2myw|2myw]]</div></td></tr> | + | </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> |
| - | <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_MAGGR Q8J180_MAGGR] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Guillen, K de]] | + | [[Category: Pyricularia grisea]] |
| - | [[Category: Kroj, T]] | + | [[Category: Kroj T]] |
| - | [[Category: Unknown function]] | + | [[Category: De Guillen K]] |
| Structural highlights
Function
Q8J180_MAGGR
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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