5W3T

Crystal structure of PopP2 in complex with IP6

Summary for 5W3T

• Entry DOI: 10.2210/pdb5w3t/pdb
• Related: 5W3X 5W3Y 5W40
• Descriptor: PopP2 protein, INOSITOL HEXAKISPHOSPHATE, GLYCEROL, ... (4 entities in total)
• Functional Keywords: yopj effector, popp2, ip6, transcription
• Biological source: Ralstonia solanacearum
• Total number of polymer chains: 4
• Total formula weight: 157618.97

Authors

Song, J.,Zhang, Z.M. (deposition date: 2017-06-08, release date: 2017-08-09, Last modification date: 2024-03-13)

Primary citation

Zhang, Z.M.,Ma, K.W.,Gao, L.,Hu, Z.,Schwizer, S.,Ma, W.,Song, J.
Mechanism of host substrate acetylation by a YopJ family effector.
Nat Plants, 3:17115-17115, 2017

PubMed Abstract: The Yersinia outer protein J (YopJ) family of bacterial effectors depends on a novel acetyltransferase domain to acetylate signalling proteins from plant and animal hosts. However, the underlying mechanism is unclear. Here, we report the crystal structures of PopP2, a YopJ effector produced by the plant pathogen Ralstonia solanacearum, in complex with inositol hexaphosphate (InsP), acetyl-coenzyme A (AcCoA) and/or substrate Resistance to Ralstonia solanacearum 1 (RRS1-R). PopP2 recognizes the WRKYGQK motif of RRS1-R to position a targeted lysine in the active site for acetylation. Importantly, the PopP2-RRS1-R association is allosterically regulated by InsP binding, suggesting a previously unidentified role of the eukaryote-specific cofactor in substrate interaction. Furthermore, we provide evidence for the reaction intermediate of PopP2-mediated acetylation, an acetyl-cysteine covalent adduct, lending direct support to the 'ping-pong'-like catalytic mechanism proposed for YopJ effectors. Our study provides critical mechanistic insights into the virulence activity of YopJ class of acetyltransferases.

PubMed: 28737762
DOI: 10.1038/nplants.2017.115

Experimental method

X-RAY DIFFRACTION (2.15 Å)