6pwg

Ewingella americana HopBF1 kinase bound to AMP-PNP

spinqualitylabelsall models 6pwg, resolution 1.89Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6pwg is a 2 chain structure with sequence from Ewingella americana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.89Å Ligands: ANP, EDO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A085GHR3_9GAMM 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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