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| | <StructureSection load='1umg' size='340' side='right'caption='[[1umg]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='1umg' size='340' side='right'caption='[[1umg]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1umg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sulto Sulto]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UMG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1UMG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1umg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfurisphaera_tokodaii_str._7 Sulfurisphaera tokodaii str. 7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UMG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UMG FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2FP:1,6-FRUCTOSE+DIPHOSPHATE+(LINEAR+FORM)'>2FP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ST0318 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273063 SULTO])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2FP:1,6-FRUCTOSE+DIPHOSPHATE+(LINEAR+FORM)'>2FP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1umg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1umg OCA], [https://pdbe.org/1umg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1umg RCSB], [https://www.ebi.ac.uk/pdbsum/1umg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1umg ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1umg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1umg OCA], [http://pdbe.org/1umg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1umg RCSB], [http://www.ebi.ac.uk/pdbsum/1umg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1umg ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/FBPAP_SULTO FBPAP_SULTO] Catalyzes two subsequent steps in gluconeogenesis: the aldol condensation of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (GA3P) to fructose-1,6-bisphosphate (FBP), and the dephosphorylation of FBP to fructose-6-phosphate (F6P).<ref>PMID:15274916</ref> <ref>PMID:20348906</ref> <ref>PMID:21983966</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Suggestions for new articles|Suggestions for new articles]] | + | *[[Fructose-1%2C6-bisphosphatase 3D structures|Fructose-1%2C6-bisphosphatase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Fructose-bisphosphatase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Sulto]] | + | [[Category: Sulfurisphaera tokodaii str. 7]] |
| - | [[Category: Fushinobu, S]] | + | [[Category: Fushinobu S]] |
| - | [[Category: Nishimasu, H]] | + | [[Category: Nishimasu H]] |
| - | [[Category: Shoun, H]] | + | [[Category: Shoun H]] |
| - | [[Category: Wakagi, T]] | + | [[Category: Wakagi T]] |
| - | [[Category: 6-bisphosphatase]]
| + | |
| - | [[Category: Alpha-beta-beta-alpha four layer sandwich]]
| + | |
| - | [[Category: Fructose-1]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Hyperthermophilic archaea]]
| + | |
| - | [[Category: Magnesium ion]]
| + | |
| - | [[Category: Octamer]]
| + | |
| - | [[Category: Phosphatase]]
| + | |
| - | [[Category: Three metal-assisted mechanism]]
| + | |
| Structural highlights
Function
FBPAP_SULTO Catalyzes two subsequent steps in gluconeogenesis: the aldol condensation of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (GA3P) to fructose-1,6-bisphosphate (FBP), and the dephosphorylation of FBP to fructose-6-phosphate (F6P).[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
As the first structure of the novel class of fructose-1,6-bisphosphatase (FBPase) present in thermophilic archaea, we solved the crystal structure of the ST0318 gene product (St-Fbp) of Sulfolobus tokodaii strain 7. The St-Fbp structure comprises a homooctamer of the 422 point-group. The protein folds as a four-layer alpha-beta-beta-alpha sandwich with a novel topology, which is completely different from the sugar phosphatase fold. The structure contains an unhydrolyzed FBP molecule in the open-keto form, as well as four hexacoordinated magnesium ions around the 1-phosphoryl group of FBP. The arrangement of the catalytic side chains and metal ligands is consistent with the three-metal ion assisted catalysis proposed for conventional FBPases. The structure provides an insight into the structural basis of the strict substrate specificity of St-Fbp.
The first crystal structure of the novel class of fructose-1,6-bisphosphatase present in thermophilic archaea.,Nishimasu H, Fushinobu S, Shoun H, Wakagi T Structure. 2004 Jun;12(6):949-59. PMID:15274916[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nishimasu H, Fushinobu S, Shoun H, Wakagi T. The first crystal structure of the novel class of fructose-1,6-bisphosphatase present in thermophilic archaea. Structure. 2004 Jun;12(6):949-59. PMID:15274916 doi:10.1016/j.str.2004.03.026
- ↑ Say RF, Fuchs G. Fructose 1,6-bisphosphate aldolase/phosphatase may be an ancestral gluconeogenic enzyme. Nature. 2010 Apr 15;464(7291):1077-81. PMID:20348906 doi:10.1038/nature08884
- ↑ Fushinobu S, Nishimasu H, Hattori D, Song HJ, Wakagi T. Structural basis for the bifunctionality of fructose-1,6-bisphosphate aldolase/phosphatase. Nature. 2011 Oct 9;478(7370):538-41. doi: 10.1038/nature10457. PMID:21983966 doi:10.1038/nature10457
- ↑ Nishimasu H, Fushinobu S, Shoun H, Wakagi T. The first crystal structure of the novel class of fructose-1,6-bisphosphatase present in thermophilic archaea. Structure. 2004 Jun;12(6):949-59. PMID:15274916 doi:10.1016/j.str.2004.03.026
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