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==CRYSTAL STRUCTURE OF THE COMPLEX OF PHOSPHOFRUCTOKINASE FROM ESCHERICHIA COLI WITH ITS REACTION PRODUCTS== | ==CRYSTAL STRUCTURE OF THE COMPLEX OF PHOSPHOFRUCTOKINASE FROM ESCHERICHIA COLI WITH ITS REACTION PRODUCTS== | ||
<StructureSection load='1pfk' size='340' side='right' caption='[[1pfk]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='1pfk' size='340' side='right' caption='[[1pfk]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=FBP:BETA-FRUCTOSE-1,6-DIPHOSPHATE'>FBP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=FBP:BETA-FRUCTOSE-1,6-DIPHOSPHATE'>FBP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=1pfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pfk OCA], [http://pdbe.org/1pfk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pfk RCSB], [http://www.ebi.ac.uk/pdbsum/1pfk 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=1pfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pfk OCA], [http://pdbe.org/1pfk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pfk RCSB], [http://www.ebi.ac.uk/pdbsum/1pfk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1pfk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pf/1pfk_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pf/1pfk_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1pfk ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1pfk" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1pfk" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 10:28, 15 February 2018
CRYSTAL STRUCTURE OF THE COMPLEX OF PHOSPHOFRUCTOKINASE FROM ESCHERICHIA COLI WITH ITS REACTION PRODUCTSCRYSTAL STRUCTURE OF THE COMPLEX OF PHOSPHOFRUCTOKINASE FROM ESCHERICHIA COLI WITH ITS REACTION PRODUCTS
Structural highlights
Function[PFKA_ECOLI] Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of Escherichia coli phosphofructokinase complexed with its reaction products fructose 1,6-bisphosphate (Fru1,6P) and ADP/Mg2+, and the allosteric activator ADP/Mg2+, has been determined at 2.4 A resolution. The structure was solved by molecular replacement using the known structure of Bacillus stearothermophilus phosphofructokinase, and has been refined to a crystallographic R-factor of 0.165 for all data. The crystallization mixture contained the substrate fructose 6-phosphate, but the electron density maps showed clearly the presence of the product fructose 1,6-bisphosphate, presumably formed by the enzyme reaction with contaminating ATP. The crystal consists of tetrameric molecules with subunits in two different conformations despite their chemical identity. The magnesium ion in the "closed" subunit bridges the phosphate groups of the two products. In the "open" subunit, the products are about 1.5 A further apart, with the Mg2+ bound only to ADP. These two conformations probably represent two successive stages along the reaction pathway, in which the closure of the subunit is required to bring the substrates sufficiently close to react. This conformational change within the subunit is distinct from the quaternary structure change seen previously in the inactive T-state conformation. It is probably not involved in the co-operativity or allosteric control of the enzyme, since the co-operative product fructose 1,6-bisphosphate is not moved, nor are the subunit interfaces changed. The structure of the enzyme is similar to that of B. stearothermophilus phosphofructokinase, and confirms the location of the sites for the two reaction products (or substrates), and of the effector site binding the activator ADP/Mg2+. However, this structure gives a clearer picture of the active site, and of the interactions between the enzyme and its reaction products. Crystal structure of the complex of phosphofructokinase from Escherichia coli with its reaction products.,Shirakihara Y, Evans PR J Mol Biol. 1988 Dec 20;204(4):973-94. PMID:2975709[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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