View source for 6pwg


==Ewingella americana HopBF1 kinase bound to AMP-PNP==
<StructureSection load='6pwg' size='340' side='right'caption='[[6pwg]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6pwg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ewingella_americana Ewingella americana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PWG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PWG 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]] 1.89&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</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=6pwg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pwg OCA], [https://pdbe.org/6pwg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pwg RCSB], [https://www.ebi.ac.uk/pdbsum/6pwg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pwg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A085GHR3_9GAMM A0A085GHR3_9GAMM] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The molecular chaperone HSP90 facilitates the folding of several client proteins, including innate immune receptors and protein kinases. HSP90 is an essential component of plant and animal immunity, yet pathogenic strategies that directly target the chaperone have not been described. Here, we identify the HopBF1 family of bacterial effectors as eukaryotic-specific HSP90 protein kinases. HopBF1 adopts a minimal protein kinase fold that is recognized by HSP90 as a host client. As a result, HopBF1 phosphorylates HSP90 to completely inhibit the chaperone's ATPase activity. We demonstrate that phosphorylation of HSP90 prevents activation of immune receptors that trigger the hypersensitive response in plants. Consequently, HopBF1-dependent phosphorylation of HSP90 is sufficient to induce severe disease symptoms in plants infected with the bacterial pathogen, Pseudomonas syringae. Collectively, our results uncover a family of bacterial effector kinases with toxin-like properties and reveal a previously unrecognized betrayal mechanism by which bacterial pathogens modulate host immunity.

A Bacterial Effector Mimics a Host HSP90 Client to Undermine Immunity.,Lopez VA, Park BC, Nowak D, Sreelatha A, Zembek P, Fernandez J, Servage KA, Gradowski M, Hennig J, Tomchick DR, Pawlowski K, Krzymowska M, Tagliabracci VS Cell. 2019 Sep 19;179(1):205-218.e21. doi: 10.1016/j.cell.2019.08.020. Epub 2019 , Sep 12. PMID:31522888<ref>PMID:31522888</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6pwg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Ewingella americana]]
[[Category: Large Structures]]
[[Category: Park BC]]
[[Category: Tagliabracci VS]]
[[Category: Tomchick DR]]