3TL8

The AvrPtoB-BAK1 complex reveals two structurally similar kinaseinteracting domains in a single type III effector

Summary for 3TL8

• Entry DOI: 10.2210/pdb3tl8/pdb
• Descriptor: BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1, Effector protein HopAB2 (3 entities in total)
• Functional Keywords: plant immunity, pseudomonas syringae, solanum lycopersicum, pamp-triggered immunity, bacterial pathogenesis, transferase-ligase complex, transferase/ligase
• Biological source: Arabidopsis thaliana (mouse-ear cress, thale-cress); More
• Cellular location: Cell membrane; Single-pass type I membrane protein: Q94F62; Secreted: Q8RSY1
• Total number of polymer chains: 8
• Total formula weight: 212576.46

Authors

Chai, J.,Cheng, W.,Gao, H. (deposition date: 2011-08-29, release date: 2012-01-11, Last modification date: 2024-10-30)

Primary citation

Cheng, W.,Munkvold, K.R.,Gao, H.,Mathieu, J.,Schwizer, S.,Wang, S.,Yan, Y.B.,Wang, J.,Martin, G.B.,Chai, J.
Structural Analysis of Pseudomonas syringae AvrPtoB Bound to Host BAK1 Reveals Two Similar Kinase-Interacting Domains in a Type III Effector.
Cell Host Microbe, 10:616-626, 2011

PubMed Abstract: To infect plants, Pseudomonas syringae pv. tomato delivers ~30 type III effector proteins into host cells, many of which interfere with PAMP-triggered immunity (PTI). One effector, AvrPtoB, suppresses PTI using a central domain to bind host BAK1, a kinase that acts with several pattern recognition receptors to activate defense signaling. A second AvrPtoB domain binds and suppresses the PTI-associated kinase Bti9 but is conversely recognized by the protein kinase Pto to activate effector-triggered immunity. We report the crystal structure of the AvrPtoB-BAK1 complex, which revealed structural similarity between these two AvrPtoB domains, suggesting that they arose by intragenic duplication. The BAK1 kinase domain is structurally similar to Pto, and a conserved region within both BAK1 and Pto interacts with AvrPtoB. BAK1 kinase activity is inhibited by AvrPtoB, and mutations at the interaction interface disrupt AvrPtoB virulence activity. These results shed light on a structural mechanism underlying host-pathogen coevolution.

PubMed: 22169508
DOI: 10.1016/j.chom.2011.10.013

Experimental method

X-RAY DIFFRACTION (2.5 Å)