View source for 6r8m


==Complex of rice blast (Magnaporthe oryzae) effector protein AVR-PikE with an engineered HMA domain of Pikp-1 from rice (Oryza sativa)==
<StructureSection load='6r8m' size='340' side='right'caption='[[6r8m]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6r8m]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryza_sativa Oryza sativa] 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=6R8M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6R8M FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></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=6r8m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r8m OCA], [https://pdbe.org/6r8m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6r8m RCSB], [https://www.ebi.ac.uk/pdbsum/6r8m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6r8m ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/D5L9G5_ORYSJ D5L9G5_ORYSJ] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Plant nucleotide binding, leucine-rich repeat (NLR) receptors detect pathogen effectors and initiate an immune response. Since their discovery, NLRs have been the focus of protein engineering to improve disease resistance. However, this approach has proven challenging, in part due to their narrow response specificity. Previously, we revealed the structural basis of pathogen recognition by the integrated heavy metal associated (HMA) domain of the rice NLR Pikp (Maqbool et al., 2015). Here, we used structure-guided engineering to expand the response profile of Pikp to variants of the rice blast pathogen effector AVR-Pik. A mutation located within an effector-binding interface of the integrated Pikp-HMA domain increased the binding affinity for AVR-Pik variants in vitro and in vivo. This translates to an expanded cell-death response to AVR-Pik variants previously unrecognized by Pikp in planta. The structures of the engineered Pikp-HMA in complex with AVR-Pik variants revealed the mechanism of expanded recognition. These results provide a proof-of-concept that protein engineering can improve the utility of plant NLR receptors where direct interaction between effectors and NLRs is established, particularly where this interaction occurs via integrated domains.

Protein engineering expands the effector recognition profile of a rice NLR immune receptor.,De la Concepcion JC, Franceschetti M, MacLean D, Terauchi R, Kamoun S, Banfield MJ Elife. 2019 Sep 19;8:e47713. doi: 10.7554/eLife.47713. PMID:31535976<ref>PMID:31535976</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6r8m" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Oryza sativa]]
[[Category: Pyricularia oryzae]]
[[Category: Banfield MJ]]
[[Category: De la Concepcion JC]]
[[Category: Franceschetti M]]