Phosphorylation-independent interaction between 14-3-3 and exoenzyme S: from structure to pathogenesis.

Phosphorylation-independent interaction between 14-3-3 and exoenzyme S: from structure to pathogenesis. Research Abstract Details 

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Phosphorylation-independent interaction between 14-3-3 and exoenzyme S: from structure to pathogenesis. Abstract Text:

Christian Ottmann,Lubna Yasmin,Michael Weyand,Jeffrey L Veesenmeyer,Maureen H Diaz,Ruth H Palmer,Matthew S Francis,Alan R Hauser,Alfred Wittinghofer,Bengt Hallberg,

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.

Phosphorylation-independent interaction between 14-3-3 and exoenzyme S: from structure to pathogenesis. Publishing Authors By Initials

C Ottmann,L Yasmin,M Weyand,JL Veesenmeyer,MH Diaz,RH Palmer,MS Francis,AR Hauser,A Wittinghofer,B Hallberg,

For similar enzymes and coenzymes: enzymes: hydrolases: acid anhydride hydrolases: gtp phosphohydrolases: gtp-binding proteins: monomeric gtp-binding proteins: rap gtp-binding proteins: rap1 gtp-binding proteins research abstracts see: enzymes and coenzymes: enzymes: hydrolases: acid anhydride hydrolases: gtp phosphohydrolases: gtp-binding proteins: monomeric gtp-binding proteins: rap gtp-binding proteins: rap1 gtp-binding proteins research

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Phosphorylation-independent interaction between 14-3-3 and exoenzyme S: from structure to pathogenesis. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: The EMBO journal

VOLUME: 26

Page Numbers: 902-13

Journal Abbreviation: EMBO J.

ISSN: 0261-4189

DAY: 18

MONTH: 01

YEAR: 2007

Phosphorylation-independent interaction between 14-3-3 and exoenzyme S: from structure to pathogenesis. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 8208664

Phosphorylation-independent interaction between 14-3-3 and exoenzyme S: from structure to pathogenesis. Keywords Mesh Terms:

KEYWORDS: rap1 GTP-Binding Proteins

MESH TERMS: metabolism

Chemical & Substance for Abstract: Phosphorylation-independent interaction between 14-3-3 and exoenzyme S: from structure to pathogenesis. Information

Substance Name: rap1 GTP-Binding Proteins

Registry Number: EC 3.6.5.2

Grant and Affiliation Information for Phosphorylation-independent interaction between 14-3-3 and exoenzyme S: from structure to pathogenesis.

AFFILIATION: Department of Structural Biology, Max-Planck-Institute for Molecular Physiology, Dortmund, Germany.

Country: England

AGENCY: United States NIAID

GRANT: AI065615

ACRONYM: AI

MEDLINETA: EMBO J

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