2ot1: Difference between revisions
New page: left|200px<br /><applet load="2ot1" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ot1, resolution 2.05Å" /> '''Fructose-1,6-bisphos... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:2ot1.gif|left|200px]]<br /><applet load="2ot1" size=" | [[Image:2ot1.gif|left|200px]]<br /><applet load="2ot1" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2ot1, resolution 2.05Å" /> | caption="2ot1, resolution 2.05Å" /> | ||
'''Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with naphthol AS-E phosphate, a competitive inhibitor'''<br /> | '''Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with naphthol AS-E phosphate, a competitive inhibitor'''<br /> | ||
| Line 7: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
2OT1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with N3P as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Fructose-bisphosphate_aldolase Fructose-bisphosphate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.13 4.1.2.13] Full crystallographic information is available from [http:// | 2OT1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with <scene name='pdbligand=N3P:'>N3P</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Fructose-bisphosphate_aldolase Fructose-bisphosphate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.13 4.1.2.13] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OT1 OCA]. | ||
==Reference== | ==Reference== | ||
| Line 22: | Line 22: | ||
[[Category: hydrophobic pocket]] | [[Category: hydrophobic pocket]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:04:50 2008'' | ||
Revision as of 16:04, 23 January 2008
|
Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with naphthol AS-E phosphate, a competitive inhibitor
OverviewOverview
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.
About this StructureAbout this Structure
2OT1 is a Single protein structure of sequence from Oryctolagus cuniculus with as ligand. Active as Fructose-bisphosphate aldolase, with EC number 4.1.2.13 Full crystallographic information is available from OCA.
ReferenceReference
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
Page seeded by OCA on Wed Jan 23 15:04:50 2008