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2o02

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{{STRUCTURE_2o02| PDB=2o02 | SCENE= }}
{{STRUCTURE_2o02| PDB=2o02 | SCENE= }}
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'''Phosphorylation independent interactions between 14-3-3 and Exoenzyme S: from structure to pathogenesis'''
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===Phosphorylation independent interactions between 14-3-3 and Exoenzyme S: from structure to pathogenesis===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_17235285}}
==About this Structure==
==About this Structure==
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[[Category: Pathogen]]
[[Category: Pathogen]]
[[Category: Protein binding/toxin complex]]
[[Category: Protein binding/toxin complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 10:08:08 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 10:48:16 2008''

Revision as of 07:48, 28 July 2008

Image:2o02.png

Template:STRUCTURE 2o02

Phosphorylation independent interactions between 14-3-3 and Exoenzyme S: from structure to pathogenesis

Template:ABSTRACT PUBMED 17235285

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 Mon Jul 28 10:48:16 2008

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