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| [[Image:1fpl.jpg|left|200px]]
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| {{Structure
| | ==FRUCTOSE-1,6-BISPHOSPHATASE (D-FRUCTOSE-1,6-BISPHOSPHATE 1-PHOSPHOHYDROLASE) COMPLEXED WITH AMP, 2,5-ANHYDRO-D-GLUCITOL-1,6-BISPHOSPHATE AND THALLIUM IONS (10 MM)== |
| |PDB= 1fpl |SIZE=350|CAPTION= <scene name='initialview01'>1fpl</scene>, resolution 2.3Å
| | <StructureSection load='1fpl' size='340' side='right'caption='[[1fpl]], [[Resolution|resolution]] 2.30Å' scene=''> |
| |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=TH1:First+Metal+Site+In+The+Monomer+Composed+Of+Chains+A'>TH1</scene>, <scene name='pdbsite=TH2:First+Metal+Site+In+The+Monomer+Composed+Of+Chains+B'>TH2</scene>, <scene name='pdbsite=TH3:Second+Metal+Site+In+The+Monomer+Composed+Of+Chains+A'>TH3</scene>, <scene name='pdbsite=TH4:Second+Metal+Site+In+The+Monomer+Composed+Of+Chains+B'>TH4</scene>, <scene name='pdbsite=TH5:Third+Metal+Site+In+The+Monomer+Composed+Of+Chains+A'>TH5</scene> and <scene name='pdbsite=TH6:Third+Metal+Site+In+The+Monomer+Composed+Of+Chains+B'>TH6</scene>
| | == Structural highlights == |
| |LIGAND= <scene name='pdbligand=AHG:2,5-ANHYDROGLUCITOL-1,6-BIPHOSPHATE'>AHG</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=TL:THALLIUM+(I)+ION'>TL</scene>
| | <table><tr><td colspan='2'>[[1fpl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FPL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FPL FirstGlance]. <br> |
| |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>
| | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| |GENE=
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AHG:2,5-ANHYDROGLUCITOL-1,6-BIPHOSPHATE'>AHG</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=TL:THALLIUM+(I)+ION'>TL</scene></td></tr> |
| |DOMAIN=
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fpl OCA], [https://pdbe.org/1fpl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fpl RCSB], [https://www.ebi.ac.uk/pdbsum/1fpl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fpl ProSAT]</span></td></tr> |
| |RELATEDENTRY=
| | </table> |
| |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fpl OCA], [http://www.ebi.ac.uk/pdbsum/1fpl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fpl RCSB]</span>
| | == Function == |
| }}
| | [https://www.uniprot.org/uniprot/F16P1_PIG F16P1_PIG] |
| | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> |
| | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fp/1fpl_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> |
| | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fpl ConSurf]. |
| | <div style="clear:both"></div> |
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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 THALLIUM IONS (10 MM)'''
| | ==See Also== |
| | | *[[Fructose-1%2C6-bisphosphatase 3D structures|Fructose-1%2C6-bisphosphatase 3D structures]] |
| | | __TOC__ |
| ==Overview== | | </StructureSection> |
| 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. | | [[Category: Large Structures]] |
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| ==About this Structure==
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| 1FPL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FPL OCA].
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| ==Reference==
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| 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:[http://www.ncbi.nlm.nih.gov/pubmed/7568043 7568043]
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| [[Category: Fructose-bisphosphatase]]
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| [[Category: Single protein]] | |
| [[Category: Sus scrofa]] | | [[Category: Sus scrofa]] |
| [[Category: Lipscomb, W N.]] | | [[Category: Lipscomb WN]] |
| [[Category: Villeret, V.]] | | [[Category: Villeret V]] |
| [[Category: carbohydrate metabolism]]
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| [[Category: hydrolase]]
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| [[Category: phosphoric monoester]]
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| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:27:46 2008''
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