1fpi

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[[Image:1fpi.jpg|left|200px]]
[[Image:1fpi.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1fpi |SIZE=350|CAPTION= <scene name='initialview01'>1fpi</scene>, resolution 2.3&Aring;
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The line below this paragraph, containing "STRUCTURE_1fpi", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Active+Site+In+The+Monomer+Composed+Of+Chains+A'>AC1</scene>, <scene name='pdbsite=AC2:Active+Site+In+The+Monomer+Composed+Of+Chains+B'>AC2</scene>, <scene name='pdbsite=AM1:Amp+Binding+Site+In+The+Monomer+Composed+Of+Chains+A'>AM1</scene>, <scene name='pdbsite=AM2:Amp+Binding+Site+In+The+Monomer+Composed+Of+Chains+B'>AM2</scene>, <scene name='pdbsite=PO1:First+Metal+Site+In+The+Monomer+Composed+Of+Chains+A'>PO1</scene>, <scene name='pdbsite=PO2:First+Metal+Site+In+The+Monomer+Composed+Of+Chains+B'>PO2</scene>, <scene name='pdbsite=PO3:Second+Metal+Site+In+The+Monomer+Composed+Of+Chains+A'>PO3</scene>, <scene name='pdbsite=PO4:Second+Metal+Site+In+The+Monomer+Composed+Of+Chains+B'>PO4</scene>, <scene name='pdbsite=PO5:Third+Metal+Site+In+The+Monomer+Composed+Of+Chains+A'>PO5</scene> and <scene name='pdbsite=PO6:Third+Metal+Site+In+The+Monomer+Composed+Of+Chains+B'>PO6</scene>
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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=AHG:2,5-ANHYDROGLUCITOL-1,6-BIPHOSPHATE'>AHG</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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=
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-->
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|DOMAIN=
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{{STRUCTURE_1fpi| PDB=1fpi | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fpi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fpi OCA], [http://www.ebi.ac.uk/pdbsum/1fpi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fpi RCSB]</span>
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}}
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'''FRUCTOSE-1,6-BISPHOSPHATASE (D-FRUCTOSE-1,6-BISPHOSPHATE 1-PHOSPHOHYDROLASE) COMPLEXED WITH AMP, 2,5-ANHYDRO-D-GLUCITOL-1,6-BISPHOSPHATE AND POTASSIUM IONS (100 MM)'''
'''FRUCTOSE-1,6-BISPHOSPHATASE (D-FRUCTOSE-1,6-BISPHOSPHATE 1-PHOSPHOHYDROLASE) COMPLEXED WITH AMP, 2,5-ANHYDRO-D-GLUCITOL-1,6-BISPHOSPHATE AND POTASSIUM IONS (100 MM)'''
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[[Category: Lipscomb, W N.]]
[[Category: Lipscomb, W N.]]
[[Category: Villeret, V.]]
[[Category: Villeret, V.]]
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[[Category: carbohydrate metabolism]]
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[[Category: Carbohydrate metabolism]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: phosphoric monoester]]
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[[Category: Phosphoric monoester]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:36:44 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:27:40 2008''
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Revision as of 13:36, 2 May 2008

Template:STRUCTURE 1fpi

FRUCTOSE-1,6-BISPHOSPHATASE (D-FRUCTOSE-1,6-BISPHOSPHATE 1-PHOSPHOHYDROLASE) COMPLEXED WITH AMP, 2,5-ANHYDRO-D-GLUCITOL-1,6-BISPHOSPHATE AND POTASSIUM IONS (100 MM)


Overview

Fructose-1,6-bisphosphatase (Fru-1,6-Pase; D-fructose-1,6-bisphosphate 1-phosphohydrolase, EC 3.1.3.11) requires two divalent metal ions to hydrolyze alpha-D-fructose 1,6-bisphosphate. Although not required for catalysis, monovalent cations modify the enzyme activity; K+ and Tl+ ions are activators, whereas Li+ ions are inhibitors. Their mechanisms of action are still unknown. We report here crystallographic structures of pig kidney Fru-1,6-Pase complexed with K+, Tl+, or both Tl+ and Li+. In the T form Fru-1,6-Pase complexed with the substrate analogue 2,5-anhydro-D-glucitol 1,6-bisphosphate (AhG-1,6-P2) and Tl+ or K+ ions, three Tl+ or K+ binding sites are found. Site 1 is defined by Glu-97, Asp-118, Asp-121, Glu-280, and a 1-phosphate oxygen of AhG-1,6-P2; site 2 is defined by Glu-97, Glu-98, Asp-118, and Leu-120. Finally, site 3 is defined by Arg-276, Glu-280, and the 1-phosphate group of AhG-1,6-P2. The Tl+ or K+ ions at sites 1 and 2 are very close to the positions previously identified for the divalent metal ions. Site 3 is specific to K+ or Tl+. In the divalent metal ion complexes, site 3 is occupied by the guanidinium group of Arg-276. These observations suggest that Tl+ or K+ ions can substitute for Arg-276 in the active site and polarize the 1-phosphate group, thus facilitating nucleophilic attack on the phosphorus center. In the T form complexed with both Tl+ and Li+ ions, Li+ replaces Tl+ at metal site 1. Inhibition by lithium very likely occurs as it binds to this site, thus retarding turnover or phosphate release. The present study provides a structural basis for a similar mechanism of inhibition for inositol monophosphatase, one of the potential targets of lithium ions in the treatment of manic depression.

About this Structure

1FPI is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.

Reference

Crystallographic evidence for the action of potassium, thallium, and lithium ions on fructose-1,6-bisphosphatase., Villeret V, Huang S, Fromm HJ, Lipscomb WN, Proc Natl Acad Sci U S A. 1995 Sep 12;92(19):8916-20. PMID:7568043 Page seeded by OCA on Fri May 2 16:36:44 2008

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