View source for 7bnt


==Complex of rice blast (Magnaporthe oryzae) effector protein AVR-PikD with a predicted ancestral HMA domain of Pik-1 from Oryza spp.==
<StructureSection load='7bnt' size='340' side='right'caption='[[7bnt]], [[Resolution|resolution]] 1.32&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7bnt]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyricularia_oryzae Pyricularia oryzae] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BNT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BNT 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]] 1.32&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=7bnt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bnt OCA], [https://pdbe.org/7bnt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bnt RCSB], [https://www.ebi.ac.uk/pdbsum/7bnt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bnt ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A subset of plant NLR immune receptors carry unconventional integrated domains in addition to their canonical domain architecture. One example is rice Pik-1 that comprises an integrated heavy metal-associated (HMA) domain. Here, we reconstructed the evolutionary history of Pik-1 and its NLR partner, Pik-2, and tested hypotheses about adaptive evolution of the HMA domain. Phylogenetic analyses revealed that the HMA domain integrated into Pik-1 before Oryzinae speciation over 15 million years ago and has been under diversifying selection. Ancestral sequence reconstruction coupled with functional studies showed that two Pik-1 allelic variants independently evolved from a weakly binding ancestral state to high-affinity binding of the blast fungus effector AVR-PikD. We conclude that for most of its evolutionary history the Pik-1 HMA domain did not sense AVR-PikD, and that different Pik-1 receptors have recently evolved through distinct biochemical paths to produce similar phenotypic outcomes. These findings highlight the dynamic nature of the evolutionary mechanisms underpinning NLR adaptation to plant pathogens.

Two NLR immune receptors acquired high-affinity binding to a fungal effector through convergent evolution of their integrated domain.,Bialas A, Langner T, Harant A, Contreras MP, Stevenson CE, Lawson DM, Sklenar J, Kellner R, Moscou MJ, Terauchi R, Banfield MJ, Kamoun S Elife. 2021 Jul 21;10:e66961. doi: 10.7554/eLife.66961. PMID:34288868<ref>PMID:34288868</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7bnt" style="background-color:#fffaf0;"></div>

==See Also==
*[[Avirulence protein 3D structures|Avirulence protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pyricularia oryzae]]
[[Category: Synthetic construct]]
[[Category: Banfield MJ]]
[[Category: Bialas A]]
[[Category: Contreras MP]]
[[Category: Harant A]]
[[Category: Kamoun S]]
[[Category: Kellner R]]
[[Category: Langner T]]
[[Category: Lawson DM]]
[[Category: Moscou MJ]]
[[Category: Sklenar J]]
[[Category: Stevenson CEM]]
[[Category: Terauchi R]]