5klq | pdb_00005klq

Crystal structure of HopZ1a in complex with IP6 and CoA

spinqualitylabelsall models 5klq, resolution 3.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5klq is a 3 chain structure with sequence from Pseudomonas syringae pv. syringae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.4Å Ligands: CIT, COA, IHP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HOZ1A_PSESY Serine/threonine-protein acetyltransferase translocated into infected cells, which impairs host microtubule network and host immunity by mediating acetylation of target proteins (PubMed:20636323, PubMed:22319451, PubMed:24204266, PubMed:27525589). Blocks secretion in host cells by mediating acetylation of host tubulin, thereby impairing host microbubule network (PubMed:22319451). Impairs host cell immunity by mediating acetylation of host TIFY/JAZ transcription repressors (Arabidopsis thaliana TIFY10B/JAZ2, TIFY11A/JAZ5, TIFY11B/JAZ6, TIFY5A/JAZ8, TIFY9/JAZ10 and TIFY3B/JAZ12), thereby activating host jasmonate signaling (PubMed:24204266, PubMed:27525589). Publication Abstract from PubMed Effectors secreted by the type III secretion system are essential for bacterial pathogenesis. Members of the Yersinia outer-protein J (YopJ) family of effectors found in diverse plant and animal pathogens depend on a protease-like catalytic triad to acetylate host proteins and produce virulence. However, the structural basis for this noncanonical acetyltransferase activity remains unknown. Here, we report the crystal structures of the YopJ effector HopZ1a, produced by the phytopathogen Pseudomonas syringae, in complex with the eukaryote-specific cofactor inositol hexakisphosphate (IP6) and/or coenzyme A (CoA). Structural, computational and functional characterizations reveal a catalytic core with a fold resembling that of ubiquitin-like cysteine proteases and an acetyl-CoA-binding pocket formed after IP6-induced structural rearrangements. Modeling-guided mutagenesis further identified key IP6-interacting residues of Salmonella effector AvrA that are required for acetylating its substrate. Our study reveals the structural basis of a novel class of acetyltransferases and the conserved allosteric regulation of YopJ effectors by IP6. Structure of a pathogen effector reveals the enzymatic mechanism of a novel acetyltransferase family.,Zhang ZM, Ma KW, Yuan S, Luo Y, Jiang S, Hawara E, Pan S, Ma W, Song J Nat Struct Mol Biol. 2016 Aug 15. doi: 10.1038/nsmb.3279. PMID:27525589 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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