8TWS

AvrB bound with UDP-rhamnose and RIN4 C-NOI motif

Summary for 8TWS

• Entry DOI: 10.2210/pdb8tws/pdb
• Related: 8TWJ 8TWO 8TXF
• Descriptor: Avirulence protein B, RPM1-interacting protein 4, [[(2~{R},3~{S},4~{R},5~{R})-5-[2,4-bis(oxidanylidene)pyrimidin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2~{R},3~{R},4~{R},5~{R},6~{S})-6-methyl-3,4,5-tris(oxidanyl)oxan-2-yl] hydrogen phosphate (3 entities in total)
• Functional Keywords: protein complex, transferase
• Biological source: Pseudomonas syringae; More
• Total number of polymer chains: 2
• Total formula weight: 40241.25

Authors

Peng, W.,Orth, K. (deposition date: 2023-08-21, release date: 2024-02-28)

Primary citation

Peng, W.,Garcia, N.,Servage, K.A.,Kohler, J.J.,Ready, J.M.,Tomchick, D.R.,Fernandez, J.,Orth, K.
Pseudomonas effector AvrB is a glycosyltransferase that rhamnosylates plant guardee protein RIN4.
Sci Adv, 10:eadd5108-eadd5108, 2024

PubMed Abstract: The plant pathogen encodes a type III secretion system avirulence effector protein, AvrB, that induces a form of programmed cell death called the hypersensitive response in plants as a defense mechanism against systemic infection. Despite the well-documented catalytic activities observed in other Fido (c, c, and AvrB) proteins, the enzymatic activity and target substrates of AvrB have remained elusive. Here, we show that AvrB is an unprecedented glycosyltransferase that transfers rhamnose from UDP-rhamnose to a threonine residue of the guardee protein RIN4. We report structures of various enzymatic states of the AvrB-catalyzed rhamnosylation reaction of RIN4, which reveal the structural and mechanistic basis for rhamnosylation by a Fido protein. Collectively, our results uncover an unexpected reaction performed by a prototypical member of the Fido superfamily while providing important insights into the plant hypersensitive response pathway and foreshadowing more diverse chemistry used by Fido proteins and their substrates.

PubMed: 38354245
DOI: 10.1126/sciadv.add5108

Experimental method

X-RAY DIFFRACTION (2.85 Å)