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1fpi

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[[Image:1fpi.jpg|left|200px]]
 
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{{Structure
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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)==
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|PDB= 1fpi |SIZE=350|CAPTION= <scene name='initialview01'>1fpi</scene>, resolution 2.3&Aring;
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<StructureSection load='1fpi' size='340' side='right'caption='[[1fpi]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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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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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene> and <scene name='pdbligand=AHG:2,5-ANHYDROGLUCITOL-1,6-BIPHOSPHATE'>AHG</scene>
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<table><tr><td colspan='2'>[[1fpi]] 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=1FPI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FPI FirstGlance]. <br>
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|ACTIVITY= [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]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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|GENE=
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<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=K:POTASSIUM+ION'>K</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fpi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fpi OCA], [https://pdbe.org/1fpi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fpi RCSB], [https://www.ebi.ac.uk/pdbsum/1fpi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fpi ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/F16P1_PIG F16P1_PIG]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fp/1fpi_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1fpi ConSurf].
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<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 POTASSIUM IONS (100 MM)'''
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==See Also==
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*[[Fructose-1%2C6-bisphosphatase 3D structures|Fructose-1%2C6-bisphosphatase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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[[Category: Large Structures]]
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==About this Structure==
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1FPI 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=1FPI 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]]
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[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
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[[Category: Lipscomb, W N.]]
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[[Category: Lipscomb WN]]
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[[Category: Villeret, V.]]
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[[Category: Villeret V]]
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[[Category: AHG]]
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[[Category: AMP]]
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[[Category: K]]
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[[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 Thu Mar 20 11:12:16 2008''
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Current revision

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)

PDB ID 1fpi

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