5jhj: Difference between revisions

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'''Unreleased structure'''


The entry 5jhj is ON HOLD  until Paper Publication
==M. Oryzae effector AVR-Pia mutant H3==
<StructureSection load='5jhj' size='340' side='right'caption='[[5jhj]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5jhj]] 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=5JHJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JHJ 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=5jhj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jhj OCA], [https://pdbe.org/5jhj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jhj RCSB], [https://www.ebi.ac.uk/pdbsum/5jhj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jhj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/R9RX08_PYROR R9RX08_PYROR]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Nucleotide binding domain and leucine-rich repeat proteins (NLRs) are important receptors in plant immunity that allow recognition of pathogen effectors. The rice (Oryza sativa) NLR RGA5 recognizes the Magnaporthe oryzae effector AVR-Pia through direct interaction. Here, we gained detailed insights into the molecular and structural bases of AVR-Pia-RGA5 interaction and the role of the RATX1 decoy domain of RGA5. NMR titration combined with in vitro and in vivo protein-protein interaction analyses identified the AVR-Pia interaction surface that binds to the RATX1 domain. Structure-informed AVR-Pia mutants showed that, although AVR-Pia associates with additional sites in RGA5, binding to the RATX1 domain is necessary for pathogen recognition but can be of moderate affinity. Therefore, RGA5-mediated resistance is highly resilient to mutations in the effector. We propose a model that explains such robust effector recognition as a consequence, and an advantage, of the combination of integrated decoy domains with additional independent effector-NLR interactions.


Authors: Padilla, A., deGuillen, K.
Recognition of the Magnaporthe oryzae Effector AVR-Pia by the Decoy Domain of the Rice NLR Immune Receptor RGA5.,Ortiz D, de Guillen K, Cesari S, Chalvon V, Gracy J, Padilla A, Kroj T Plant Cell. 2017 Jan;29(1):156-168. doi: 10.1105/tpc.16.00435. Epub 2017 Jan 13. PMID:28087830<ref>PMID:28087830</ref>


Description: M. Oryzae effector AVR-Pia mutant H3
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Deguillen, K]]
<div class="pdbe-citations 5jhj" style="background-color:#fffaf0;"></div>
[[Category: Padilla, A]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pyricularia oryzae]]
[[Category: Padilla A]]
[[Category: DeGuillen K]]
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