View source for 7xvi


==pathogen effectors which are essential to cause plant disease by manipulating cellular processes in the host==
<StructureSection load='7xvi' size='340' side='right'caption='[[7xvi]], [[Resolution|resolution]] 3.11&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7xvi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Phytophthora_infestans Phytophthora infestans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XVI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XVI 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]] 3.11&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <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=7xvi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xvi OCA], [https://pdbe.org/7xvi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xvi RCSB], [https://www.ebi.ac.uk/pdbsum/7xvi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xvi ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A833T3B4_PHYIN A0A833T3B4_PHYIN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Pathogens produce diverse effector proteins to manipulate host cellular processes. However, how functional diversity is generated in an effector repertoire is poorly understood. Many effectors in the devastating plant pathogen Phytophthora contain tandem repeats of the "(L)WY" motif, which are structurally conserved but variable in sequences. Here, we discovered a functional module formed by a specific (L)WY-LWY combination in multiple Phytophthora effectors, which efficiently recruits the serine/threonine protein phosphatase 2A (PP2A) core enzyme in plant hosts. Crystal structure of an effector-PP2A complex shows that the (L)WY-LWY module enables hijacking of the host PP2A core enzyme to form functional holoenzymes. While sharing the PP2A-interacting module at the amino terminus, these effectors possess divergent C-terminal LWY units and regulate distinct sets of phosphoproteins in the host. Our results highlight the appropriation of an essential host phosphatase through molecular mimicry by pathogens and diversification promoted by protein modularity in an effector repertoire.

Pathogen protein modularity enables elaborate mimicry of a host phosphatase.,Li H, Wang J, Kuan TA, Tang B, Feng L, Wang J, Cheng Z, Sklenar J, Derbyshire P, Hulin M, Li Y, Zhai Y, Hou Y, Menke FLH, Wang Y, Ma W Cell. 2023 Jul 20;186(15):3196-3207.e17. doi: 10.1016/j.cell.2023.05.049. Epub , 2023 Jun 26. PMID:37369204<ref>PMID:37369204</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7xvi" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Phytophthora infestans]]
[[Category: Wang J]]
[[Category: Wang Y]]