1o9c

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[[Image:1o9c.gif|left|200px]]
[[Image:1o9c.gif|left|200px]]
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{{Structure
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|PDB= 1o9c |SIZE=350|CAPTION= <scene name='initialview01'>1o9c</scene>, resolution 2.60&Aring;
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|SITE= <scene name='pdbsite=FLC:Flc+Binding+Site+For+Chain+A'>FLC</scene>
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>
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{{STRUCTURE_1o9c| PDB=1o9c | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1o9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o9c OCA], [http://www.ebi.ac.uk/pdbsum/1o9c PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1o9c RCSB]</span>
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'''STRUCTURAL VIEW OF A FUNGAL TOXIN ACTING ON A 14-3-3 REGULATORY COMPLEX'''
'''STRUCTURAL VIEW OF A FUNGAL TOXIN ACTING ON A 14-3-3 REGULATORY COMPLEX'''
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[[Category: Wurtele, M.]]
[[Category: Wurtele, M.]]
[[Category: 14-3-3 family]]
[[Category: 14-3-3 family]]
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[[Category: activating drug]]
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[[Category: Activating drug]]
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[[Category: fusicoccin]]
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[[Category: Fusicoccin]]
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[[Category: plant plasma membrane (h+)atpase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:33:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:41:50 2008''
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Revision as of 00:33, 3 May 2008

Template:STRUCTURE 1o9c

STRUCTURAL VIEW OF A FUNGAL TOXIN ACTING ON A 14-3-3 REGULATORY COMPLEX


Overview

The fungal phytotoxin fusicoccin stabilizes the interaction between the C-terminus of the plant plasma membrane H(+)-ATPase and 14-3-3 proteins, thus leading to permanent activation of the proton pump. This results in an irreversible opening of the stomatal pore, followed by wilting of plants. Here, we report the crystal structure of the ternary complex between a plant 14-3-3 protein, fusicoccin and a phosphopeptide derived from the C-terminus of the H(+)-ATPase. Comparison with the corresponding binary 14-3-3 complexes indicates no major conformational change induced by fusicoccin. The compound rather fills a cavity in the protein-phosphopeptide interaction surface. Isothermal titration calorimetry indicates that the toxin alone binds only weakly to 14-3-3 and that peptide and toxin mutually increase each others' binding affinity approximately 90-fold. These results are important for herbicide development but might have general implications for drug development, since rather than inhibiting protein-protein interactions, which is difficult to accomplish, it might be easier to reverse the strategy and stabilize protein-protein complexes. As the fusicoccin interaction shows, only low-affinity interactions would be required for this strategy.

About this Structure

1O9C is a Single protein structure of sequence from Nicotiana tabacum. Full crystallographic information is available from OCA.

Reference

Structural view of a fungal toxin acting on a 14-3-3 regulatory complex., Wurtele M, Jelich-Ottmann C, Wittinghofer A, Oecking C, EMBO J. 2003 Mar 3;22(5):987-94. PMID:12606564 Page seeded by OCA on Sat May 3 03:33:03 2008

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