1fpl: Difference between revisions

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-[[Image:1fpl.gif|left|200px]]<br />
-<applet load="1fpl" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1fpl, resolution 2.3&Aring;" />
-'''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)'''<br />
-==Overview==
+==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)==
-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 ... [[http://ispc.weizmann.ac.il/pmbin/getpm?7568043 (full description)]]
+<StructureSection load='1fpl' size='340' side='right'caption='[[1fpl]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+== Structural highlights ==
+<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>
+</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>
+<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>
+<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>
+</table>
+== 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>
-==About this Structure==
+==See Also==
-FPL is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]] with TL, AMP and AHG as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[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]]. Structure known Active Sites: AC1, AC2, AM1, AM2, TH1, TH2, TH3, TH4, TH5 and TH6. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FPL OCA]].
+*[[Fructose-1%2C6-bisphosphatase 3D structures|Fructose-1%2C6-bisphosphatase 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-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://ispc.weizmann.ac.il//pmbin/getpm?pmid=7568043 7568043]
+[[Category: Large Structures]]
-[[Category: Fructose-bisphosphatase]]
-[[Category: Single protein]]
 [[Category: Sus scrofa]]
-[[Category: Lipscomb, W.N.]]
+[[Category: Lipscomb WN]]
-[[Category: Villeret, V.]]
+[[Category: Villeret V]]
-[[Category: AHG]]
-[[Category: AMP]]
-[[Category: TL]]
-[[Category: carbohydrate metabolism]]
-[[Category: hydrolase]]
-[[Category: phosphoric monoester]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:50:55 2007''