1r5e
From Proteopedia
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| - | [[Image:1r5e.jpg|left|200px]] | + | [[Image:1r5e.jpg|left|200px]] |
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| - | '''Solution structure of the folded core of Pseudomonas syringae effector protein, AvrPto''' | + | {{Structure |
| + | |PDB= 1r5e |SIZE=350|CAPTION= <scene name='initialview01'>1r5e</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Solution structure of the folded core of Pseudomonas syringae effector protein, AvrPto''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1R5E is a [ | + | 1R5E is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_syringae Pseudomonas syringae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R5E OCA]. |
==Reference== | ==Reference== | ||
| - | The solution structure of type III effector protein AvrPto reveals conformational and dynamic features important for plant pathogenesis., Wulf J, Pascuzzi PE, Fahmy A, Martin GB, Nicholson LK, Structure. 2004 Jul;12(7):1257-68. PMID:[http:// | + | The solution structure of type III effector protein AvrPto reveals conformational and dynamic features important for plant pathogenesis., Wulf J, Pascuzzi PE, Fahmy A, Martin GB, Nicholson LK, Structure. 2004 Jul;12(7):1257-68. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15242602 15242602] |
[[Category: Pseudomonas syringae]] | [[Category: Pseudomonas syringae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: three-helix bundle]] | [[Category: three-helix bundle]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:47:05 2008'' |
Revision as of 11:47, 20 March 2008
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Solution structure of the folded core of Pseudomonas syringae effector protein, AvrPto
Overview
Pseudomonas syringae pv. tomato, the causative agent of bacterial speck disease of tomato, uses a type III secretion system (TTSS) to deliver effector proteins into the host cell. In resistant plants, the bacterial effector protein AvrPto physically interacts with the host Pto kinase and elicits antibacterial defense responses. In susceptible plants, which lack the Pto kinase, AvrPto acts as a virulence factor to promote bacterial growth. The solution structure of AvrPto reveals a functional core consisting of a three-helix bundle motif flanked by disordered N- and C-terminal tails. Residues required for Pto binding lie in a 19 residue Omega loop. Modeling suggests a hydrophobic patch involving the activation loop of Pto forms a contact surface with the AvrPto Omega loop and that helix packing mediates interactions between AvrPto and putative virulence targets Api2 and Api3. The AvrPto structure has a low stability that may facilitate chaperone-independent secretion by the TTSS.
About this Structure
1R5E is a Single protein structure of sequence from Pseudomonas syringae. Full crystallographic information is available from OCA.
Reference
The solution structure of type III effector protein AvrPto reveals conformational and dynamic features important for plant pathogenesis., Wulf J, Pascuzzi PE, Fahmy A, Martin GB, Nicholson LK, Structure. 2004 Jul;12(7):1257-68. PMID:15242602
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