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==The AvrPtoB-BAK1 complex reveals two structurally similar kinaseinteracting domains in a single type III effector== | |||
<StructureSection load='3tl8' size='340' side='right' caption='[[3tl8]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3tl8]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] and [http://en.wikipedia.org/wiki/Pseudomonas_syringae_pv._tomato Pseudomonas syringae pv. tomato]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TL8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TL8 FirstGlance]. <br> | |||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BAK1, ELG, SERK3, At4g33430, F17M5.190 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana]), hopAB2, avrPtoB, PSPTO_3087 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=323 Pseudomonas syringae pv. tomato])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3tl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tl8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tl8 RCSB], [http://www.ebi.ac.uk/pdbsum/3tl8 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:22169508</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Avirulence protein|Avirulence protein]] | *[[Avirulence protein|Avirulence protein]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Arabidopsis thaliana]] | [[Category: Arabidopsis thaliana]] | ||
[[Category: Pseudomonas syringae pv. tomato]] | [[Category: Pseudomonas syringae pv. tomato]] | ||
[[Category: Chai, J | [[Category: Chai, J]] | ||
[[Category: Cheng, W | [[Category: Cheng, W]] | ||
[[Category: Gao, H | [[Category: Gao, H]] | ||
[[Category: Bacterial pathogenesis]] | [[Category: Bacterial pathogenesis]] | ||
[[Category: Pamp-triggered immunity]] | [[Category: Pamp-triggered immunity]] | ||
Revision as of 11:35, 18 December 2014
The AvrPtoB-BAK1 complex reveals two structurally similar kinaseinteracting domains in a single type III effectorThe AvrPtoB-BAK1 complex reveals two structurally similar kinaseinteracting domains in a single type III effector
Structural highlights
Publication Abstract from PubMedTo 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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