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| | <StructureSection load='3n1c' size='340' side='right'caption='[[3n1c]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='3n1c' size='340' side='right'caption='[[3n1c]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3n1c]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N1C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3N1C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3n1c]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N1C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3N1C FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</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]] 2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3cqd|3cqd]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b1723, JW5280, PFK2, pfkB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/6-phosphofructokinase 6-phosphofructokinase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3n1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n1c OCA], [https://pdbe.org/3n1c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3n1c RCSB], [https://www.ebi.ac.uk/pdbsum/3n1c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3n1c ProSAT]</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=3n1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n1c OCA], [https://pdbe.org/3n1c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3n1c RCSB], [https://www.ebi.ac.uk/pdbsum/3n1c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3n1c ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/PFKB_ECOLI PFKB_ECOLI] Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.<ref>PMID:16866375</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 6-phosphofructokinase]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Ecoli]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Babul, J]] | + | [[Category: Babul J]] |
| - | [[Category: Cabrera, R]] | + | [[Category: Cabrera R]] |
| - | [[Category: Caniuguir, A]] | + | [[Category: Caniuguir A]] |
| - | [[Category: Garratt, R C]] | + | [[Category: Garratt RC]] |
| - | [[Category: Pereira, H M]] | + | [[Category: Pereira HM]] |
| - | [[Category: Escherichia coli]]
| + | |
| - | [[Category: Glycolysis]]
| + | |
| - | [[Category: Pfk-2]]
| + | |
| - | [[Category: Phosphofructokinase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
PFKB_ECOLI Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.[1]
Publication Abstract from PubMed
Substrate inhibition by ATP is a regulatory feature of the phosphofructokinases isoenzymes from E. coli (Pfk-1 and Pfk-2). Under gluconeogenic conditions, the loss of this regulation in Pfk-2 causes substrate cycling of fructose-6-P and futile consumption of ATP delaying growth. In the present work we have broached the mechanism of ATP-induced inhibition of Pfk-2 from both structural and kinetic perspectives. The crystal structure of Pfk-2 in complex with fructose-6-P is reported to a resolution of 2 A. The comparison of this structure with the previously reported inhibited form of the enzyme suggests a negative interplay between fructose-6-P binding and allosteric binding of MgATP. Initial velocity experiments show a linear increase of the apparent K0.5 for fructose-6-P and a decrease in the apparent kcat as a function of MgATP concentration. These effects occur simultaneously with the induction of a sigmoidal kinetic behavior (nH approx. 2). Differences and resemblances in the patterns of fructose-6-P binding and the mechanism of inhibition are discussed for Pfk-1 and Pfk-2, as an example of evolutionary convergence, since these enzymes do not share a common ancestor.
The crystal complex of phosphofructokinase-2 of Escherichia coli with fructose-6-P: kinetic and structural analysis of the allosteric ATP inhibition.,Cabrera R, Baez M, Pereira HM, Caniuguir A, Garratt RC, Babul J J Biol Chem. 2010 Dec 8. PMID:21147773[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Parducci RE, Cabrera R, Baez M, Guixé V. Evidence for a catalytic Mg2+ ion and effect of phosphate on the activity of Escherichia coli phosphofructokinase-2: regulatory properties of a ribokinase family member. Biochemistry. 2006 Aug 1;45(30):9291-9. PMID:16866375 doi:10.1021/bi060026o
- ↑ Cabrera R, Baez M, Pereira HM, Caniuguir A, Garratt RC, Babul J. The crystal complex of phosphofructokinase-2 of Escherichia coli with fructose-6-P: kinetic and structural analysis of the allosteric ATP inhibition. J Biol Chem. 2010 Dec 8. PMID:21147773 doi:10.1074/jbc.M110.163162
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