| Structural highlights
3tl8 is a 8 chain structure with sequence from Arabidopsis thaliana and Pseudomonas syringae pv. tomato. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | NonStd Res: | |
| Gene: | BAK1, ELG, SERK3, At4g33430, F17M5.190 (Arabidopsis thaliana), hopAB2, avrPtoB, PSPTO_3087 (Pseudomonas syringae pv. tomato) |
| Resources: | FirstGlance, OCA, RCSB, PDBsum |
Function
[HPAB2_PSESM] Effector protein involved in gene-for-gene resistance in tomato plants. It is recognized by the host Pto resistance protein and elicits Pto and Prf-dependent hypersensitive response (HR) and programmed cell death (PCD), resulting in host immunity. In susceptible plants, acts as a virulence factor by suppressing PCD and HR-based plant immunity. This function requires its E3 ubiquitin ligase activity probably by recruiting E2 enzymes and transferring ubiquitin molecules to cellular proteins involved in regulation of PCD and targeting them for degradation. Also, induces expression of host genes involved in ethylene biosynthesis and signaling, in particular ACO1 and ACO2, encoding the ethylene-forming enzyme ACC oxidase.[1] [2] [3] [4] [5]
Publication Abstract from PubMed
To infect plants, Pseudomonas syringae pv. tomato delivers approximately 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.
Structural Analysis of Pseudomonas syringae AvrPtoB Bound to Host BAK1 Reveals Two Similar Kinase-Interacting Domains in a Type III Effector.,Cheng W, Munkvold KR, Gao H, Mathieu J, Schwizer S, Wang S, Yan YB, Wang J, Martin GB, Chai J Cell Host Microbe. 2011 Dec 15;10(6):616-26. Epub 2011 Dec 8. PMID:22169508[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kim YJ, Lin NC, Martin GB. Two distinct Pseudomonas effector proteins interact with the Pto kinase and activate plant immunity. Cell. 2002 May 31;109(5):589-98. PMID:12062102
- ↑ Abramovitch RB, Kim YJ, Chen S, Dickman MB, Martin GB. Pseudomonas type III effector AvrPtoB induces plant disease susceptibility by inhibition of host programmed cell death. EMBO J. 2003 Jan 2;22(1):60-9. PMID:12505984 doi:http://dx.doi.org/10.1093/emboj/cdg006
- ↑ Cohn JR, Martin GB. Pseudomonas syringae pv. tomato type III effectors AvrPto and AvrPtoB promote ethylene-dependent cell death in tomato. Plant J. 2005 Oct;44(1):139-54. PMID:16167902 doi:http://dx.doi.org/TPJ2516
- ↑ Abramovitch RB, Janjusevic R, Stebbins CE, Martin GB. Type III effector AvrPtoB requires intrinsic E3 ubiquitin ligase activity to suppress plant cell death and immunity. Proc Natl Acad Sci U S A. 2006 Feb 21;103(8):2851-6. Epub 2006 Feb 13. PMID:16477026 doi:http://dx.doi.org/0507892103
- ↑ Janjusevic R, Abramovitch RB, Martin GB, Stebbins CE. A bacterial inhibitor of host programmed cell death defenses is an E3 ubiquitin ligase. Science. 2006 Jan 13;311(5758):222-6. Epub 2005 Dec 22. PMID:16373536 doi:http://dx.doi.org/1120131
- ↑ Cheng W, Munkvold KR, Gao H, Mathieu J, Schwizer S, Wang S, Yan YB, Wang J, Martin GB, 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. 2011 Dec 15;10(6):616-26. Epub 2011 Dec 8. PMID:22169508 doi:10.1016/j.chom.2011.10.013
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