2o02
From Proteopedia
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|PDB= 2o02 |SIZE=350|CAPTION= <scene name='initialview01'>2o02</scene>, resolution 1.500Å | |PDB= 2o02 |SIZE=350|CAPTION= <scene name='initialview01'>2o02</scene>, resolution 1.500Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=BEZ:BENZOIC ACID'>BEZ</scene> | + | |LIGAND= <scene name='pdbligand=BEZ:BENZOIC+ACID'>BEZ</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= YWHAZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= YWHAZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2o02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o02 OCA], [http://www.ebi.ac.uk/pdbsum/2o02 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2o02 RCSB]</span> | ||
}} | }} | ||
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[[Category: Wittinghofer, A.]] | [[Category: Wittinghofer, A.]] | ||
[[Category: Yasmin, L.]] | [[Category: Yasmin, L.]] | ||
| - | [[Category: BEZ]] | ||
[[Category: 14-3-3]] | [[Category: 14-3-3]] | ||
[[Category: adapter protein]] | [[Category: adapter protein]] | ||
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[[Category: protein binding/toxin complex]] | [[Category: protein binding/toxin complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:10:55 2008'' |
Revision as of 01:10, 31 March 2008
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| , resolution 1.500Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | YWHAZ (Homo sapiens) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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