2ot0: Difference between revisions

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[[Image:2ot0.jpg|left|200px]]
{{Seed}}
[[Image:2ot0.png|left|200px]]


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{{STRUCTURE_2ot0|  PDB=2ot0  |  SCENE=  }}  
{{STRUCTURE_2ot0|  PDB=2ot0  |  SCENE=  }}  


'''Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with a C-terminal peptide of Wiskott-Aldrich syndrome protein'''
===Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with a C-terminal peptide of Wiskott-Aldrich syndrome protein===




==Overview==
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Aldolase plays essential catalytic roles in glycolysis and gluconeogenesis. However, aldolase is a highly abundant protein that is remarkably promiscuous in its interactions with other cellular proteins. In particular, aldolase binds to highly acidic amino acid sequences, including the C terminus of the Wiskott-Aldrich syndrome protein, an actin nucleation-promoting factor. Here we report the crystal structure of tetrameric rabbit muscle aldolase in complex with a C-terminal peptide of Wiskott-Aldrich syndrome protein. Aldolase recognizes a short, four-residue DEWD motif (residues 498-501), which adopts a loose hairpin turn that folds around the central aromatic residue, enabling its tryptophan side chain to fit into a hydrophobic pocket in the active site of aldolase. The flanking acidic residues in this binding motif provide further interactions with conserved aldolase active site residues Arg-42 and Arg-303, aligning their side chains and forming the sides of the hydrophobic pocket. The binding of Wiskott-Aldrich syndrome protein to aldolase precludes intramolecular interactions of its C terminus with its active site and is competitive with substrate as well as with binding by actin and cortactin. Finally, based on this structure, a novel naphthol phosphate-based inhibitor of aldolase was identified, and its structure in complex with aldolase demonstrated mimicry of the Wiskott-Aldrich syndrome protein-aldolase interaction. The data support a model whereby aldolase exists in distinct forms that regulate glycolysis or actin dynamics.
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{{ABSTRACT_PUBMED_17329259}}


==About this Structure==
==About this Structure==
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[[Category: Hydrophobic pocket]]
[[Category: Hydrophobic pocket]]
[[Category: Wasp]]
[[Category: Wasp]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 11:35:59 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:20:52 2008''

Revision as of 03:20, 29 July 2008

File:2ot0.png

Template:STRUCTURE 2ot0

Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with a C-terminal peptide of Wiskott-Aldrich syndrome protein

Template:ABSTRACT PUBMED 17329259

About this Structure

2OT0 is a Protein complex structure of sequences from Oryctolagus cuniculus. Full crystallographic information is available from OCA.

Reference

A hydrophobic pocket in the active site of glycolytic aldolase mediates interactions with Wiskott-Aldrich syndrome protein., St-Jean M, Izard T, Sygusch J, J Biol Chem. 2007 May 11;282(19):14309-15. Epub 2007 Feb 27. PMID:17329259

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