2o02
From Proteopedia
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'''Phosphorylation independent interactions between 14-3-3 and Exoenzyme S: from structure to pathogenesis''' | '''Phosphorylation independent interactions between 14-3-3 and Exoenzyme S: from structure to pathogenesis''' | ||
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[[Category: Yasmin, L.]] | [[Category: Yasmin, L.]] | ||
[[Category: 14-3-3]] | [[Category: 14-3-3]] | ||
| - | [[Category: | + | [[Category: Adapter protein]] |
| - | [[Category: | + | [[Category: Exo]] |
| - | [[Category: | + | [[Category: Pathogen]] |
| - | [[Category: | + | [[Category: Protein binding/toxin complex]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 10:08:08 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 07:08, 4 May 2008
Phosphorylation independent interactions between 14-3-3 and Exoenzyme S: from structure to pathogenesis
Overview
14-3-3 proteins are phosphoserine/phosphothreonine-recognizing adapter proteins that regulate the activity of a vast array of targets. There are also examples of 14-3-3 proteins binding their targets via unphosphorylated motifs. Here we present a structural and biological investigation of the phosphorylation-independent interaction between 14-3-3 and exoenzyme S (ExoS), an ADP-ribosyltransferase toxin of Pseudomonas aeruginosa. ExoS binds to 14-3-3 in a novel binding mode mostly relying on hydrophobic contacts. The 1.5 A crystal structure is supported by cytotoxicity analysis, which reveals that substitution of the corresponding hydrophobic residues significantly weakens the ability of ExoS to modify the endogenous targets RAS/RAP1 and to induce cell death. Furthermore, mutation of key residues within the ExoS binding site for 14-3-3 impairs virulence in a mouse pneumonia model. In conclusion, we show that ExoS binds 14-3-3 in a novel reversed orientation that is primarily dependent on hydrophobic residues. This interaction is phosphorylation independent and is required for the function of ExoS.
About this Structure
2O02 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Phosphorylation-independent interaction between 14-3-3 and exoenzyme S: from structure to pathogenesis., Ottmann C, Yasmin L, Weyand M, Veesenmeyer JL, Diaz MH, Palmer RH, Francis MS, Hauser AR, Wittinghofer A, Hallberg B, EMBO J. 2007 Feb 7;26(3):902-13. Epub 2007 Jan 18. PMID:17235285 Page seeded by OCA on Sun May 4 10:08:08 2008
