2fd4
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fd4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fd4 OCA], [http://www.ebi.ac.uk/pdbsum/2fd4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fd4 RCSB]</span> | ||
}} | }} | ||
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[[Category: ubiquitin ligase]] | [[Category: ubiquitin ligase]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:01:09 2008'' |
Revision as of 00:01, 31 March 2008
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, resolution 1.80Å | |||||||
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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
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