View source for 2myw


==Solution structure of M. oryzae protein AVR-PIA==
<StructureSection load='2myw' size='340' side='right'caption='[[2myw]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2myw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyricularia_oryzae Pyricularia oryzae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MYW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MYW FirstGlance]. <br>
</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'>[https://proteopedia.org/fgij/fg.htm?mol=2myw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2myw OCA], [https://pdbe.org/2myw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2myw RCSB], [https://www.ebi.ac.uk/pdbsum/2myw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2myw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B9WZW9_PYROR B9WZW9_PYROR] 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:26506000</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2myw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pyricularia oryzae]]
[[Category: Kroj T]]
[[Category: De Guillen K]]