2fd4: Difference between revisions
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'''Crystal Structure of AvrPtoB (436-553)''' | '''Crystal Structure of AvrPtoB (436-553)''' | ||
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[[Category: Janjusevic, R.]] | [[Category: Janjusevic, R.]] | ||
[[Category: Stebbins, C E.]] | [[Category: Stebbins, C E.]] | ||
[[Category: | [[Category: Avrptob]] | ||
[[Category: | [[Category: Pseudomona]] | ||
[[Category: | [[Category: Ring finger]] | ||
[[Category: | [[Category: U-box]] | ||
[[Category: | [[Category: Ubiquitin ligase]] | ||
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Revision as of 00:45, 4 May 2008
Crystal Structure of AvrPtoB (436-553)
Overview
The Pseudomonas syringae protein AvrPtoB is translocated into plant cells, where it inhibits immunity-associated programmed cell death (PCD). The structure of a C-terminal domain of AvrPtoB that is essential for anti-PCD activity reveals an unexpected homology to the U-box and RING-finger components of eukaryotic E3 ubiquitin ligases, and we show that AvrPtoB has ubiquitin ligase activity. Mutation of conserved residues involved in the binding of E2 ubiquitin-conjugating enzymes abolishes this activity in vitro, as well as anti-PCD activity in tomato leaves, which dramatically decreases virulence. These results show that Pseudomonas syringae uses a mimic of host E3 ubiquitin ligases to inactivate plant defenses.
About this Structure
2FD4 is a Single protein structure of sequence from Pseudomonas syringae. Full crystallographic information is available from OCA.
Reference
A bacterial inhibitor of host programmed cell death defenses is an E3 ubiquitin ligase., Janjusevic R, Abramovitch RB, Martin GB, Stebbins CE, Science. 2006 Jan 13;311(5758):222-6. Epub 2005 Dec 22. PMID:16373536 Page seeded by OCA on Sun May 4 03:45:04 2008
