5KLP

Crystal structure of HopZ1a in complex with IP6

Summary for 5KLP

• Entry DOI: 10.2210/pdb5klp/pdb
• Related: 5KLQ
• Descriptor: Orf34, INOSITOL HEXAKISPHOSPHATE, CITRIC ACID, ... (4 entities in total)
• Functional Keywords: ser/thr acetyltransferase, transferase
• Biological source: Pseudomonas syringae pv. syringae
• Total number of polymer chains: 3
• Total formula weight: 117722.53

Authors

Zhang, Z.-M.,Song, J. (deposition date: 2016-06-24, release date: 2016-08-10, Last modification date: 2024-10-23)

Primary citation

Zhang, Z.M.,Ma, K.W.,Yuan, S.,Luo, Y.,Jiang, S.,Hawara, E.,Pan, S.,Ma, W.,Song, J.
Structure of a pathogen effector reveals the enzymatic mechanism of a novel acetyltransferase family.
Nat.Struct.Mol.Biol., 23:847-852, 2016

PubMed Abstract: 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.

PubMed: 27525589
DOI: 10.1038/nsmb.3279

Experimental method

X-RAY DIFFRACTION (2.002 Å)