2myv: Difference between revisions

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~~'''Unreleased structure'''~~

~~The entry~~ 2myv is ~~ON HOLD~~

==Solution structure of M. oryzae protein AVR1-CO39==

== Structural highlights ==

<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='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=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>

== Function ==

[https://www.uniprot.org/uniprot/Q8J180_PYRGI 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.

~~Authors:~~ de Guillen, K.

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>

~~Description~~: ~~Solution structure of Fungus protein Q8J180_MAGGR~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased~~ Structures]]

</div>

[[Category: De Guillen, K]]

== References ==

__TOC__

</StructureSection>

[[Category: Large Structures]]

[[Category: Pyricularia grisea]]

[[Category: Kroj T]]

[[Category: De Guillen K]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 2myv is ON HOLD
+==Solution structure of M. oryzae protein AVR1-CO39==
+<StructureSection load='2myv' size='340' side='right'caption='[[2myv]]' scene=''>
+== Structural highlights ==
+<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='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=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>
+== Function ==
+[https://www.uniprot.org/uniprot/Q8J180_PYRGI Q8J180_PYRGI]
+<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.
-Authors: de Guillen, K.
+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>
-Description: Solution structure of Fungus protein Q8J180_MAGGR
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: De Guillen, K]]
+<div class="pdbe-citations 2myv" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Pyricularia grisea]]
+[[Category: Kroj T]]
+[[Category: De Guillen K]]