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2o02

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[[Image:2o02.jpg|left|200px]]<br /><applet load="2o02" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2o02.jpg|left|200px]]
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caption="2o02, resolution 1.500&Aring;" />
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'''Phosphorylation independent interactions between 14-3-3 and Exoenzyme S: from structure to pathogenesis'''<br />
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{{Structure
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|PDB= 2o02 |SIZE=350|CAPTION= <scene name='initialview01'>2o02</scene>, resolution 1.500&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=BEZ:BENZOIC ACID'>BEZ</scene>
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|ACTIVITY=
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|GENE= YWHAZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''Phosphorylation independent interactions between 14-3-3 and Exoenzyme S: from structure to pathogenesis'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2O02 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=BEZ:'>BEZ</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O02 OCA].
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2O02 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O02 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17235285 17235285]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17235285 17235285]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: 14-3-3]]
[[Category: 14-3-3]]
[[Category: adapter protein]]
[[Category: adapter protein]]
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[[Category: exos]]
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[[Category: exo]]
[[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 Thu Feb 21 18:13:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:53:23 2008''

Revision as of 15:53, 20 March 2008


PDB ID 2o02

Drag the structure with the mouse to rotate
, resolution 1.500Å
Ligands:
Gene: YWHAZ (Homo sapiens)
Coordinates: save as pdb, mmCIF, xml



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

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