2o02
From Proteopedia
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- | [[Image:2o02.jpg|left|200px]] | + | [[Image:2o02.jpg|left|200px]] |
- | + | ||
- | '''Phosphorylation independent interactions between 14-3-3 and Exoenzyme S: from structure to pathogenesis''' | + | {{Structure |
+ | |PDB= 2o02 |SIZE=350|CAPTION= <scene name='initialview01'>2o02</scene>, resolution 1.500Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=BEZ:BENZOIC ACID'>BEZ</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= YWHAZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
+ | }} | ||
+ | |||
+ | '''Phosphorylation independent interactions between 14-3-3 and Exoenzyme S: from structure to pathogenesis''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 2O02 is a [ | + | 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== | ||
- | 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:// | + | 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]] | ||
- | [[Category: | + | [[Category: exo]] |
[[Category: pathogen]] | [[Category: pathogen]] | ||
[[Category: protein binding/toxin complex]] | [[Category: protein binding/toxin complex]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''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
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, resolution 1.500Å | |||||||
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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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