2o02

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[[Image:2o02.jpg|left|200px]]
 
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{{Structure
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==Phosphorylation independent interactions between 14-3-3 and Exoenzyme S: from structure to pathogenesis==
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|PDB= 2o02 |SIZE=350|CAPTION= <scene name='initialview01'>2o02</scene>, resolution 1.500&Aring;
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<StructureSection load='2o02' size='340' side='right'caption='[[2o02]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=BEZ:BENZOIC ACID'>BEZ</scene>
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<table><tr><td colspan='2'>[[2o02]] is a 4 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O02 FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
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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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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEZ:BENZOIC+ACID'>BEZ</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2o02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o02 OCA], [https://pdbe.org/2o02 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o02 RCSB], [https://www.ebi.ac.uk/pdbsum/2o02 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o02 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/1433Z_HUMAN 1433Z_HUMAN] Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner.<ref>PMID:9360956</ref> <ref>PMID:14578935</ref> <ref>PMID:15071501</ref> <ref>PMID:15644438</ref> <ref>PMID:16376338</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o0/2o02_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2o02 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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'''Phosphorylation independent interactions between 14-3-3 and Exoenzyme S: from structure to pathogenesis'''
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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:17235285<ref>PMID:17235285</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2o02" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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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*[[14-3-3 protein 3D structures|14-3-3 protein 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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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].
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__TOC__
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</StructureSection>
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==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://www.ncbi.nlm.nih.gov/pubmed/17235285 17235285]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Hallberg, B.]]
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[[Category: Hallberg B]]
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[[Category: Hauser, A R.]]
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[[Category: Hauser AR]]
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[[Category: Ottmann, C.]]
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[[Category: Ottmann C]]
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[[Category: Weyand, M.]]
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[[Category: Weyand M]]
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[[Category: Wittinghofer, A.]]
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[[Category: Wittinghofer A]]
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[[Category: Yasmin, L.]]
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[[Category: Yasmin L]]
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[[Category: BEZ]]
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[[Category: 14-3-3]]
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[[Category: adapter protein]]
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[[Category: exo]]
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[[Category: pathogen]]
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[[Category: protein binding/toxin complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:53:23 2008''
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Current revision

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

PDB ID 2o02

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