View source for 3n1c


==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]] 2.00&Aring;' scene=''>
== Structural highlights ==
<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>
<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=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='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>
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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3n1c" style="background-color:#fffaf0;"></div>

==See Also==
*[[Phosphofructokinase (PFK)|Phosphofructokinase (PFK)]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: 6-phosphofructokinase]]
[[Category: Ecoli]]
[[Category: Babul, J]]
[[Category: Cabrera, R]]
[[Category: Caniuguir, A]]
[[Category: Garratt, R C]]
[[Category: Pereira, H M]]
[[Category: Escherichia coli]]
[[Category: Glycolysis]]
[[Category: Pfk-2]]
[[Category: Phosphofructokinase]]
[[Category: Transferase]]