5jhj: Difference between revisions
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New page: '''Unreleased structure''' The entry 5jhj is ON HOLD until Paper Publication Authors: Padilla, A., deGuillen, K. Description: M. Oryzae effector AVR-Pia mutant H3 [[Category: Unrelease... |
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==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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5jhj" style="background-color:#fffaf0;"></div> | ||
[[Category: Padilla | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pyricularia oryzae]] | |||
[[Category: Padilla A]] | |||
[[Category: DeGuillen K]] | |||
Latest revision as of 08:42, 9 October 2024
M. Oryzae effector AVR-Pia mutant H3
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