3n1c: Difference between revisions
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==Crystal structure of the phosphofructokinase-2 from Escherichia coli in complex with fructose-6-phosphate== | ==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=''> | <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 [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3n1c]] is a 4 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3N1C 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></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></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3cqd|3cqd]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3cqd|3cqd]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b1723, JW5280, PFK2, pfkB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b1723, JW5280, PFK2, pfkB ([http://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'>[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=3n1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n1c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3n1c RCSB], [http://www.ebi.ac.uk/pdbsum/3n1c 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=3n1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n1c OCA], [http://pdbe.org/3n1c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3n1c RCSB], [http://www.ebi.ac.uk/pdbsum/3n1c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3n1c ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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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 3n1c" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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</StructureSection> | </StructureSection> | ||
[[Category: 6-phosphofructokinase]] | [[Category: 6-phosphofructokinase]] | ||
[[Category: | [[Category: Ecoli]] | ||
[[Category: Babul, J]] | [[Category: Babul, J]] | ||
[[Category: Cabrera, R]] | [[Category: Cabrera, R]] | ||
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[[Category: Garratt, R C]] | [[Category: Garratt, R C]] | ||
[[Category: Pereira, H M]] | [[Category: Pereira, H M]] | ||
[[Category: Escherichia coli]] | |||
[[Category: Glycolysis]] | [[Category: Glycolysis]] | ||
[[Category: Pfk-2]] | [[Category: Pfk-2]] | ||
[[Category: Phosphofructokinase]] | [[Category: Phosphofructokinase]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 06:49, 10 December 2016
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
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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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