2qkw
From Proteopedia
(New page: 200px<br /><applet load="2qkw" size="350" color="white" frame="true" align="right" spinBox="true" caption="2qkw, resolution 3.20Å" /> '''Structural basis for...) |
|||
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
| - | Pathogenic microbes use effectors to enhance susceptibility in host | + | Pathogenic microbes use effectors to enhance susceptibility in host plants. However, plants have evolved a sophisticated immune system to detect these effectors using cognate disease resistance proteins, a recognition that is highly specific, often elicits rapid and localized cell death, known as a hypersensitive response, and thus potentially limits pathogen growth. Despite numerous genetic and biochemical studies on the interactions between pathogen effector proteins and plant resistance proteins, the structural bases for such interactions remain elusive. The direct interaction between the tomato protein kinase Pto and the Pseudomonas syringae effector protein AvrPto is known to trigger disease resistance and programmed cell death through the nucleotide-binding site/leucine-rich repeat (NBS-LRR) class of disease resistance protein Prf. Here we present the crystal structure of an AvrPto-Pto complex. Contrary to the widely held hypothesis that AvrPto activates Pto kinase activity, our structural and biochemical analyses demonstrated that AvrPto is an inhibitor of Pto kinase in vitro. The AvrPto-Pto interaction is mediated by the phosphorylation-stabilized P+1 loop and a second loop in Pto, both of which negatively regulate the Prf-mediated defences in the absence of AvrPto in tomato plants. Together, our results show that AvrPto derepresses host defences by interacting with the two defence-inhibition loops of Pto. |
==About this Structure== | ==About this Structure== | ||
| Line 15: | Line 15: | ||
[[Category: Pseudomonas syringae]] | [[Category: Pseudomonas syringae]] | ||
[[Category: Solanum pimpinellifolium]] | [[Category: Solanum pimpinellifolium]] | ||
| - | [[Category: Chai, J | + | [[Category: Chai, J J.]] |
[[Category: Hao, Q.]] | [[Category: Hao, Q.]] | ||
[[Category: Liu, Q.]] | [[Category: Liu, Q.]] | ||
| - | [[Category: Xing, W | + | [[Category: Xing, W M.]] |
| - | [[Category: Zhou, J | + | [[Category: Zhou, J M.]] |
[[Category: Zou, Y.]] | [[Category: Zou, Y.]] | ||
[[Category: avrpto-pto duplex]] | [[Category: avrpto-pto duplex]] | ||
| Line 28: | Line 28: | ||
[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:40:05 2008'' |
Revision as of 16:40, 21 February 2008
|
Structural basis for activation of plant immunity by bacterial effector protein AvrPto
Overview
Pathogenic microbes use effectors to enhance susceptibility in host plants. However, plants have evolved a sophisticated immune system to detect these effectors using cognate disease resistance proteins, a recognition that is highly specific, often elicits rapid and localized cell death, known as a hypersensitive response, and thus potentially limits pathogen growth. Despite numerous genetic and biochemical studies on the interactions between pathogen effector proteins and plant resistance proteins, the structural bases for such interactions remain elusive. The direct interaction between the tomato protein kinase Pto and the Pseudomonas syringae effector protein AvrPto is known to trigger disease resistance and programmed cell death through the nucleotide-binding site/leucine-rich repeat (NBS-LRR) class of disease resistance protein Prf. Here we present the crystal structure of an AvrPto-Pto complex. Contrary to the widely held hypothesis that AvrPto activates Pto kinase activity, our structural and biochemical analyses demonstrated that AvrPto is an inhibitor of Pto kinase in vitro. The AvrPto-Pto interaction is mediated by the phosphorylation-stabilized P+1 loop and a second loop in Pto, both of which negatively regulate the Prf-mediated defences in the absence of AvrPto in tomato plants. Together, our results show that AvrPto derepresses host defences by interacting with the two defence-inhibition loops of Pto.
About this Structure
2QKW is a Protein complex structure of sequences from Pseudomonas syringae and Solanum pimpinellifolium. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.
Reference
The structural basis for activation of plant immunity by bacterial effector protein AvrPto., Xing W, Zou Y, Liu Q, Liu J, Luo X, Huang Q, Chen S, Zhu L, Bi R, Hao Q, Wu JW, Zhou JM, Chai J, Nature. 2007 Sep 13;449(7159):243-7. Epub 2007 Aug 12. PMID:17694048
Page seeded by OCA on Thu Feb 21 18:40:05 2008
Categories: Non-specific serine/threonine protein kinase | Protein complex | Pseudomonas syringae | Solanum pimpinellifolium | Chai, J J. | Hao, Q. | Liu, Q. | Xing, W M. | Zhou, J M. | Zou, Y. | Avrpto-pto duplex | Kinase | Layered beta-sheets | Serine/threonine-protein kinase | Three-helix bundle motif | Transferase
