3n1c: Difference between revisions
New page: '''Unreleased structure''' The entry 3n1c is ON HOLD until sometime in the future Authors: Pereira, H.M., Cabrera, R., Caniuguir, A., Garratt, R.C., Babul, J. Description: Crystal Stru... |
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The | ==Crystal structure of the phosphofructokinase-2 from Escherichia coli in complex with fructose-6-phosphate== | ||
<StructureSection load='3n1c' size='340' side='right'caption='[[3n1c]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<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='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='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='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> | |||
== 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;"> | |||
== 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<ref>PMID:21147773</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3n1c" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Phosphofructokinase 3D structures|Phosphofructokinase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli K-12]] | |||
[[Category: Large Structures]] | |||
[[Category: Babul J]] | |||
[[Category: Cabrera R]] | |||
[[Category: Caniuguir A]] | |||
[[Category: Garratt RC]] | |||
[[Category: Pereira HM]] | |||
Latest revision as of 12:06, 6 September 2023
Crystal structure of the phosphofructokinase-2 from Escherichia coli in complex with fructose-6-phosphateCrystal structure of the phosphofructokinase-2 from Escherichia coli in complex with fructose-6-phosphate
Structural highlights
FunctionPFKB_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 PubMedSubstrate 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 AlsoReferences
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