2q8m

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[[Image:2q8m.jpg|left|200px]]
[[Image:2q8m.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 2q8m |SIZE=350|CAPTION= <scene name='initialview01'>2q8m</scene>, resolution 2.050&Aring;
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The line below this paragraph, containing "STRUCTURE_2q8m", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=BG6:BETA-D-GLUCOSE-6-PHOSPHATE'>BG6</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FBP:FRUCTOSE-1,6-DIPHOSPHATE'>FBP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Fructose-bisphosphatase Fructose-bisphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.11 3.1.3.11] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= fbp ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=621 Shigella boydii])
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-->
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|DOMAIN=
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{{STRUCTURE_2q8m| PDB=2q8m | SCENE= }}
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|RELATEDENTRY=[[2gq1|2GQ1]], [[2owz|2OWZ]], [[2ox3|2OX3]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2q8m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q8m OCA], [http://www.ebi.ac.uk/pdbsum/2q8m PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2q8m RCSB]</span>
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}}
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'''T-like Fructose-1,6-bisphosphatase from Escherichia coli with AMP, Glucose 6-phosphate, and Fructose 1,6-bisphosphate bound'''
'''T-like Fructose-1,6-bisphosphatase from Escherichia coli with AMP, Glucose 6-phosphate, and Fructose 1,6-bisphosphate bound'''
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[[Category: Honzatko, R B.]]
[[Category: Honzatko, R B.]]
[[Category: Kruesel, C E.]]
[[Category: Kruesel, C E.]]
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[[Category: allosteric regulation]]
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[[Category: Allosteric regulation]]
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[[Category: bacteria]]
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[[Category: Bacteria]]
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[[Category: carbohydrate metabolism]]
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[[Category: Carbohydrate metabolism]]
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[[Category: diabetes]]
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[[Category: Diabetes]]
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[[Category: gluconeogenesis]]
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[[Category: Gluconeogenesis]]
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[[Category: glycolysis]]
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[[Category: Glycolysis]]
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[[Category: gram-negative]]
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[[Category: Gram-negative]]
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[[Category: heterotrophic]]
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[[Category: Heterotrophic]]
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[[Category: protein crystallography]]
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[[Category: Protein crystallography]]
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[[Category: protein-protein interaction]]
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[[Category: Protein-protein interaction]]
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[[Category: proteobacteria]]
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[[Category: Proteobacteria]]
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[[Category: x-ray diffraction]]
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[[Category: X-ray diffraction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 14:32:28 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:46:17 2008''
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Revision as of 11:32, 4 May 2008

Image:2q8m.jpg

Template:STRUCTURE 2q8m

T-like Fructose-1,6-bisphosphatase from Escherichia coli with AMP, Glucose 6-phosphate, and Fructose 1,6-bisphosphate bound


Overview

Allosteric activation of fructose-1,6-bisphosphatase (FBPase) from Escherichia coli by phosphoenolpyruvate implies rapid feed-forward activation of gluconeogenesis in heterotrophic bacteria. But how do such bacteria rapidly down-regulate an activated FBPase in order to avoid futile cycling? Demonstrated here is the allosteric inhibition of E. coli FBPase by glucose 6-phosphate (Glc-6-P), the first metabolite produced upon glucose transport into the cell. FBPase undergoes a quaternary transition from the canonical R-state to a T-like state in response to Glc-6-P and AMP ligation. By displacing Phe(15), AMP binds to an allosteric site comparable with that of mammalian FBPase. Relative movements in helices H1 and H2 perturb allosteric activator sites for phosphoenolpyruvate. Glc-6-P binds to allosteric sites heretofore not observed in previous structures, perturbing subunits that in pairs form complete active sites of FBPase. Glc-6-P and AMP are synergistic inhibitors of E. coli FBPase, placing AMP/Glc-6-P inhibition in bacteria as a possible evolutionary predecessor to AMP/fructose 2,6-bisphosphate inhibition in mammalian FBPases. With no exceptions, signature residues of allosteric activation appear in bacterial sequences along with key residues of the Glc-6-P site. FBPases in such organisms may be components of metabolic switches that allow rapid changeover between gluconeogenesis and glycolysis in response to nutrient availability.

About this Structure

2Q8M is a Single protein structure of sequence from Shigella boydii. Full crystallographic information is available from OCA.

Reference

Structure of inhibited fructose-1,6-bisphosphatase from Escherichia coli: distinct allosteric inhibition sites for AMP and glucose 6-phosphate and the characterization of a gluconeogenic switch., Hines JK, Kruesel CE, Fromm HJ, Honzatko RB, J Biol Chem. 2007 Aug 24;282(34):24697-706. Epub 2007 Jun 13. PMID:17567577 Page seeded by OCA on Sun May 4 14:32:28 2008

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