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| | ==M. Oryzae effector AVR-Pia mutant H3== | | ==M. Oryzae effector AVR-Pia mutant H3== |
| - | <StructureSection load='5jhj' size='340' side='right'caption='[[5jhj]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='5jhj' size='340' side='right'caption='[[5jhj]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5jhj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpi_841383_[[magnaporthe_oryzae]] Bpi 841383 [[magnaporthe 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JHJ FirstGlance]. <br> | + | <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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AVR-Pia ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=318829 BPI 841383 [[Magnaporthe oryzae]]])</td></tr> | + | </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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5jhj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jhj OCA], [http://pdbe.org/5jhj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jhj RCSB], [http://www.ebi.ac.uk/pdbsum/5jhj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jhj 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=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> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/R9RX08_PYROR R9RX08_PYROR] |
| | <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: Padilla, A]] | + | [[Category: Pyricularia oryzae]] |
| - | [[Category: DeGuillen, K]]
| + | [[Category: Padilla A]] |
| - | [[Category: Avirulence effector magnaporthe oryzae]]
| + | [[Category: DeGuillen K]] |
| - | [[Category: Rga5-binding protein]] | + | |
| - | [[Category: Structure from molmol]] | + | |
| - | [[Category: Unknown function]]
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| Structural highlights
Function
R9RX08_PYROR
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ortiz D, de Guillen K, Cesari S, Chalvon V, Gracy J, Padilla A, Kroj T. Recognition of the Magnaporthe oryzae Effector AVR-Pia by the Decoy Domain of the Rice NLR Immune Receptor RGA5. Plant Cell. 2017 Jan;29(1):156-168. doi: 10.1105/tpc.16.00435. Epub 2017 Jan 13. PMID:28087830 doi:http://dx.doi.org/10.1105/tpc.16.00435
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