6fub

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==Complex of rice blast (Magnaporthe oryzae) effector protein AVR-PikE with the HMA domain of Pikm-1 from rice (Oryza sativa)==
==Complex of rice blast (Magnaporthe oryzae) effector protein AVR-PikE with the HMA domain of Pikm-1 from rice (Oryza sativa)==
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<StructureSection load='6fub' size='340' side='right' caption='[[6fub]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
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<StructureSection load='6fub' size='340' side='right'caption='[[6fub]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6fub]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FUB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FUB FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6fub]] 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=6FUB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6FUB FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6fu9|6fu9]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3&#8491;</td></tr>
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<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=6fub FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fub OCA], [http://pdbe.org/6fub PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fub RCSB], [http://www.ebi.ac.uk/pdbsum/6fub PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fub ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6fub FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fub OCA], [https://pdbe.org/6fub PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fub RCSB], [https://www.ebi.ac.uk/pdbsum/6fub PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6fub ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/C4B8C2_PYROR C4B8C2_PYROR]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Accelerated adaptive evolution is a hallmark of plant-pathogen interactions. Plant intracellular immune receptors (NLRs) often occur as allelic series with differential pathogen specificities. The determinants of this specificity remain largely unknown. Here, we unravelled the biophysical and structural basis of expanded specificity in the allelic rice NLR Pik, which responds to the effector AVR-Pik from the rice blast pathogen Magnaporthe oryzae. Rice plants expressing the Pikm allele resist infection by blast strains expressing any of three AVR-Pik effector variants, whereas those expressing Pikp only respond to one. Unlike Pikp, the integrated heavy metal-associated (HMA) domain of Pikm binds with high affinity to each of the three recognized effector variants, and variation at binding interfaces between effectors and Pikp-HMA or Pikm-HMA domains encodes specificity. By understanding how co-evolution has shaped the response profile of an allelic NLR, we highlight how natural selection drove the emergence of new receptor specificities. This work has implications for the engineering of NLRs with improved utility in agriculture.
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Polymorphic residues in rice NLRs expand binding and response to effectors of the blast pathogen.,De la Concepcion JC, Franceschetti M, Maqbool A, Saitoh H, Terauchi R, Kamoun S, Banfield MJ Nat Plants. 2018 Jul 9. pii: 10.1038/s41477-018-0194-x. doi:, 10.1038/s41477-018-0194-x. PMID:29988155<ref>PMID:29988155</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6fub" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Banfield, M J]]
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[[Category: Large Structures]]
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[[Category: Concepcion, J C.De la]]
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[[Category: Oryza sativa Japonica Group]]
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[[Category: Franceschetti, M]]
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[[Category: Pyricularia oryzae]]
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[[Category: Antifungal protein]]
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[[Category: Banfield MJ]]
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[[Category: Complex]]
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[[Category: De la Concepcion JC]]
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[[Category: Fungal effector]]
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[[Category: Franceschetti M]]
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[[Category: Plant immunity]]
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[[Category: Plant nlr]]
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Current revision

Complex of rice blast (Magnaporthe oryzae) effector protein AVR-PikE with the HMA domain of Pikm-1 from rice (Oryza sativa)

PDB ID 6fub

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