|
|
| Line 1: |
Line 1: |
| | + | |
| | ==Structure of phosphofructokinase from Saccharomyces cerevisiae== | | ==Structure of phosphofructokinase from Saccharomyces cerevisiae== |
| | <StructureSection load='3o8o' size='340' side='right' caption='[[3o8o]], [[Resolution|resolution]] 2.90Å' scene=''> | | <StructureSection load='3o8o' size='340' side='right' caption='[[3o8o]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3o8o]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O8O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3O8O FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3o8o]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O8O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3O8O FirstGlance]. <br> |
| | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene>, <scene name='pdbligand=FDP:FRUCTOSE-2,6-DIPHOSPHATE'>FDP</scene></td></tr> | | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene>, <scene name='pdbligand=FDP:FRUCTOSE-2,6-DIPHOSPHATE'>FDP</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PFK1, YGR240C, G8599 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]), PFK2, YMR205C, YM8325.06C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PFK1, YGR240C, G8599 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), PFK2, YMR205C, YM8325.06C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr> |
| | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/6-phosphofructokinase 6-phosphofructokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.11 2.7.1.11] </span></td></tr> | | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/6-phosphofructokinase 6-phosphofructokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.11 2.7.1.11] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3o8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o8o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3o8o RCSB], [http://www.ebi.ac.uk/pdbsum/3o8o PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3o8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o8o OCA], [http://pdbe.org/3o8o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3o8o RCSB], [http://www.ebi.ac.uk/pdbsum/3o8o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3o8o ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/K6PF1_YEAST K6PF1_YEAST]] Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.[HAMAP-Rule:MF_03184]<ref>PMID:11221662</ref> <ref>PMID:147195</ref> <ref>PMID:3000145</ref> <ref>PMID:3007939</ref> <ref>PMID:6211191</ref> <ref>PMID:6219673</ref> <ref>PMID:8132627</ref> <ref>PMID:8663166</ref> [[http://www.uniprot.org/uniprot/K6PF2_YEAST K6PF2_YEAST]] Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.[HAMAP-Rule:MF_03184]<ref>PMID:11221662</ref> <ref>PMID:3000145</ref> <ref>PMID:3007939</ref> <ref>PMID:40590</ref> <ref>PMID:6211191</ref> <ref>PMID:6219673</ref> <ref>PMID:8132627</ref> <ref>PMID:8663166</ref> | + | [[http://www.uniprot.org/uniprot/PFKA1_YEAST PFKA1_YEAST]] Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.[HAMAP-Rule:MF_03184]<ref>PMID:11221662</ref> <ref>PMID:147195</ref> <ref>PMID:3000145</ref> <ref>PMID:3007939</ref> <ref>PMID:6211191</ref> <ref>PMID:6219673</ref> <ref>PMID:8132627</ref> <ref>PMID:8663166</ref> [[http://www.uniprot.org/uniprot/PFKA2_YEAST PFKA2_YEAST]] Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.[HAMAP-Rule:MF_03184]<ref>PMID:11221662</ref> <ref>PMID:3000145</ref> <ref>PMID:3007939</ref> <ref>PMID:40590</ref> <ref>PMID:6211191</ref> <ref>PMID:6219673</ref> <ref>PMID:8132627</ref> <ref>PMID:8663166</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 18: |
Line 19: |
| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 3o8o" style="background-color:#fffaf0;"></div> |
| | | | |
| | ==See Also== | | ==See Also== |
| Line 26: |
Line 28: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: 6-phosphofructokinase]] | | [[Category: 6-phosphofructokinase]] |
| - | [[Category: Saccharomyces cerevisiae]] | + | [[Category: Atcc 18824]] |
| | [[Category: Banaszak, K]] | | [[Category: Banaszak, K]] |
| | [[Category: Kopperschlager, G]] | | [[Category: Kopperschlager, G]] |
| Structural highlights
3o8o is a 8 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , |
| Gene: | PFK1, YGR240C, G8599 (ATCC 18824), PFK2, YMR205C, YM8325.06C (ATCC 18824) |
| Activity: | 6-phosphofructokinase, with EC number 2.7.1.11 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[PFKA1_YEAST] Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.[HAMAP-Rule:MF_03184][1] [2] [3] [4] [5] [6] [7] [8] [PFKA2_YEAST] Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.[HAMAP-Rule:MF_03184][9] [10] [11] [12] [13] [14] [15] [16]
Publication Abstract from PubMed
Phosphofructokinase 1 (PFK) is a multisubunit allosteric enzyme that catalyzes the principal regulatory step in glycolysis-the phosphorylation of fructose 6-phosphate to fructose 1,6-bisphosphate by ATP. The activity of eukaryotic PFK is modulated by a number of effectors in response to the cell's needs for energy and building blocks for biosynthesis. The crystal structures of eukaryotic PFKs-from Saccharomyces cerevisiae and rabbit skeletal muscle-demonstrate how successive gene duplications and fusion are reflected in the protein structure and how they allow the evolution of new functionalities. The basic framework inherited from prokaryotes is conserved, and additional levels of structural and functional complexity have evolved around it. Analysis of protein-ligand complexes has shown how PFK is activated by fructose 2,6-bisphosphate (a powerful PFK effector found only in eukaryotes) and reveals a novel nucleotide binding site. Crystallographic results have been used as the basis for structure-based effector design.
The Crystal Structures of Eukaryotic Phosphofructokinases from Baker's Yeast and Rabbit Skeletal Muscle.,Banaszak K, Mechin I, Obmolova G, Oldham M, Chang SH, Ruiz T, Radermacher M, Kopperschlager G, Rypniewski W J Mol Biol. 2011 Jan 15. PMID:21241708[17]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Rodicio R, Strauss A, Heinisch JJ. Single point mutations in either gene encoding the subunits of the heterooctameric yeast phosphofructokinase abolish allosteric inhibition by ATP. J Biol Chem. 2000 Dec 29;275(52):40952-60. PMID:11221662
- ↑ Clifton D, Weinstock SB, Fraenkel DG. Glycolysis mutants in Saccharomyces cerevisiae. Genetics. 1978 Jan;88(1):1-11. PMID:147195
- ↑ Hofmann E, Eschrich K, Schellenberger W. Temporal organization of the phosphofructokinase/fructose-1,6-biphosphatase cycle. Adv Enzyme Regul. 1985;23:331-62. PMID:3000145
- ↑ Heinisch J. Isolation and characterization of the two structural genes coding for phosphofructokinase in yeast. Mol Gen Genet. 1986 Jan;202(1):75-82. PMID:3007939
- ↑ Clifton D, Fraenkel DG. Mutant studies of yeast phosphofructokinase. Biochemistry. 1982 Apr 13;21(8):1935-42. PMID:6211191
- ↑ Nissler K, Otto A, Schellenberger W, Hofmann E. Similarity of activation of yeast phosphofructokinase by AMP and fructose-2,6-bisphosphate. Biochem Biophys Res Commun. 1983 Feb 28;111(1):294-300. PMID:6219673
- ↑ Arvanitidis A, Heinisch JJ. Studies on the function of yeast phosphofructokinase subunits by in vitro mutagenesis. J Biol Chem. 1994 Mar 25;269(12):8911-8. PMID:8132627
- ↑ Heinisch JJ, Boles E, Timpel C. A yeast phosphofructokinase insensitive to the allosteric activator fructose 2,6-bisphosphate. Glycolysis/metabolic regulation/allosteric control. J Biol Chem. 1996 Jul 5;271(27):15928-33. PMID:8663166
- ↑ Rodicio R, Strauss A, Heinisch JJ. Single point mutations in either gene encoding the subunits of the heterooctameric yeast phosphofructokinase abolish allosteric inhibition by ATP. J Biol Chem. 2000 Dec 29;275(52):40952-60. PMID:11221662
- ↑ Hofmann E, Eschrich K, Schellenberger W. Temporal organization of the phosphofructokinase/fructose-1,6-biphosphatase cycle. Adv Enzyme Regul. 1985;23:331-62. PMID:3000145
- ↑ Heinisch J. Isolation and characterization of the two structural genes coding for phosphofructokinase in yeast. Mol Gen Genet. 1986 Jan;202(1):75-82. PMID:3007939
- ↑ Navon G, Shulman RG, Yamane T, Eccleshall TR, Lam KB, Baronofsky JJ, Marmur J. Phosphorus-31 nuclear magnetic resonance studies of wild-type and glycolytic pathway mutants of Saccharomyces cerevisiae. Biochemistry. 1979 Oct 16;18(21):4487-99. PMID:40590
- ↑ Clifton D, Fraenkel DG. Mutant studies of yeast phosphofructokinase. Biochemistry. 1982 Apr 13;21(8):1935-42. PMID:6211191
- ↑ Nissler K, Otto A, Schellenberger W, Hofmann E. Similarity of activation of yeast phosphofructokinase by AMP and fructose-2,6-bisphosphate. Biochem Biophys Res Commun. 1983 Feb 28;111(1):294-300. PMID:6219673
- ↑ Arvanitidis A, Heinisch JJ. Studies on the function of yeast phosphofructokinase subunits by in vitro mutagenesis. J Biol Chem. 1994 Mar 25;269(12):8911-8. PMID:8132627
- ↑ Heinisch JJ, Boles E, Timpel C. A yeast phosphofructokinase insensitive to the allosteric activator fructose 2,6-bisphosphate. Glycolysis/metabolic regulation/allosteric control. J Biol Chem. 1996 Jul 5;271(27):15928-33. PMID:8663166
- ↑ Banaszak K, Mechin I, Obmolova G, Oldham M, Chang SH, Ruiz T, Radermacher M, Kopperschlager G, Rypniewski W. The Crystal Structures of Eukaryotic Phosphofructokinases from Baker's Yeast and Rabbit Skeletal Muscle. J Mol Biol. 2011 Jan 15. PMID:21241708 doi:10.1016/j.jmb.2011.01.019
|
