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| | <StructureSection load='6q76' size='340' side='right'caption='[[6q76]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='6q76' size='340' side='right'caption='[[6q76]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6q76]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpi_841383_[[magnaporthe_oryzae]] Bpi 841383 [[magnaporthe oryzae]]] and [http://en.wikipedia.org/wiki/Japanese_rice Japanese rice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q76 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6Q76 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6q76]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryza_sativa_Japonica_Group Oryza sativa Japonica Group] and [https://en.wikipedia.org/wiki/Pyricularia_oryzae Pyricularia oryzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q76 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Q76 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Pikp-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=39947 Japanese rice]), 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">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</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=6q76 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q76 OCA], [http://pdbe.org/6q76 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6q76 RCSB], [http://www.ebi.ac.uk/pdbsum/6q76 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6q76 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=6q76 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q76 OCA], [https://pdbe.org/6q76 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6q76 RCSB], [https://www.ebi.ac.uk/pdbsum/6q76 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6q76 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/E9KPB5_ORYSJ E9KPB5_ORYSJ] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Japanese rice]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Banfield, M J]] | + | [[Category: Oryza sativa Japonica Group]] |
| - | [[Category: Varden, F A]] | + | [[Category: Pyricularia oryzae]] |
| - | [[Category: Antifungal protein]] | + | [[Category: Banfield MJ]] |
| - | [[Category: Effector]] | + | [[Category: Varden FA]] |
| - | [[Category: Heavy metal-associated]]
| + | |
| - | [[Category: Max]]
| + | |
| - | [[Category: Nlr]]
| + | |
| Structural highlights
Function
E9KPB5_ORYSJ
Publication Abstract from PubMed
Unconventional integrated domains in plant intracellular immune receptors of the nucleotide-binding leucine-rich repeat (NLRs) type can directly bind translocated effector proteins from pathogens and thereby initiate an immune response. The rice (Oryza sativa) immune receptor pairs Pik-1/Pik-2 and RGA5/RGA4 both use integrated heavy metal-associated (HMA) domains to bind the effectors AVR-Pik and AVR-Pia, respectively, from the rice blast fungal pathogen Magnaporthe oryzae. These effectors both belong to the MAX effector family and share a core structural fold, despite being divergent in sequence. How integrated domains in NLRs maintain specificity of effector recognition, even of structurally similar effectors, has implications for understanding plant immune receptor evolution and function. Here, using plant cell death and pathogenicity assays and protein-protein interaction analyses, we show that the rice NLR pair Pikp-1/Pikp-2 triggers an immune response leading to partial disease resistance towards the "mis-matched" effector AVR-Pia in planta, and that the Pikp-HMA domain binds AVR-Pia in vitro. We observed that the HMA domain from another Pik-1 allele, Pikm, cannot bind AVR-Pia, and does not trigger a plant response. The crystal structure of Pikp-HMA bound to AVR-Pia at 1.9 A resolution revealed a binding interface different from those formed with AVR-Pik effectors, suggesting plasticity in integrated domain-effector interactions. The results of our work indicate that a single NLR immune receptor can bait multiple pathogen effectors via an integrated domain, insights that may enable engineering plant immune receptors with extended disease resistance profiles.
Cross-reactivity of a rice NLR immune receptor to distinct effectors from the rice blast pathogen Magnaporthe oryzae provides partial disease resistance.,Varden FA, Saitoh H, Yoshino K, Franceschetti M, Kamoun S, Terauchi R, Banfield MJ J Biol Chem. 2019 Jul 11. pii: RA119.007730. doi: 10.1074/jbc.RA119.007730. PMID:31296569[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Varden FA, Saitoh H, Yoshino K, Franceschetti M, Kamoun S, Terauchi R, Banfield MJ. Cross-reactivity of a rice NLR immune receptor to distinct effectors from the rice blast pathogen Magnaporthe oryzae provides partial disease resistance. J Biol Chem. 2019 Jul 11. pii: RA119.007730. doi: 10.1074/jbc.RA119.007730. PMID:31296569 doi:http://dx.doi.org/10.1074/jbc.RA119.007730
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