3pfk: Difference between revisions

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PHOSPHOFRUCTOKINASE. STRUCTURE AND CONTROL

OverviewOverview

Phosphofructokinase from Bacillus stearothermophilus shows cooperative kinetics with respect to the substrate fructose-6-phosphate (F6P), allosteric activation by ADP, and inhibition by phosphoenolpyruvate. The crystal structure of the active conformation of the enzyme has been solved to 2.4 A resolution, and three ligand-binding sites have been located. Two of these form the active site and bind the substrates F6P and ATP. The third site binds both allosteric activator and inhibitor. The complex of the enzyme with F6P and ADP has been partly refined at 2.4 A resolution, and a model of ATP has been built into the active site by using the refined model of ADP and a 6 A resolution map of bound 5'-adenylylimidodiphosphate (AMPPNP). The gamma-phosphate of ATP is close to the 1-hydroxyl of F6P, in a suitable position for in-line phosphoryl transfer. The binding of the phosphate of F6P involves two arginines from a neighbouring subunit in the tetramer, which suggests that a rearrangement of the subunits could explain the cooperativity of substrate binding. The activatory ADP is also bound by residues from two subunits.

About this StructureAbout this Structure

3PFK is a Single protein structure of sequence from Geobacillus stearothermophilus with as ligand. Active as 6-phosphofructokinase, with EC number 2.7.1.11 Full crystallographic information is available from OCA.

ReferenceReference

Phosphofructokinase: structure and control., Evans PR, Farrants GW, Hudson PJ, Philos Trans R Soc Lond B Biol Sci. 1981 Jun 26;293(1063):53-62. PMID:6115424

Page seeded by OCA on Thu Feb 21 19:10:46 2008

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OCA

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-[[Image:3pfk.gif|left|200px]]<br /><applet load="3pfk" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:3pfk.gif|left|200px]]<br /><applet load="3pfk" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="3pfk, resolution 2.4&Aring;" />
 '''PHOSPHOFRUCTOKINASE. STRUCTURE AND CONTROL'''<br />
 ==Overview==
-Phosphofructokinase from Bacillus stearothermophilus shows cooperative, kinetics with respect to the substrate fructose-6-phosphate (F6P), allosteric activation by ADP, and inhibition by phosphoenolpyruvate. The, crystal structure of the active conformation of the enzyme has been solved, to 2.4 A resolution, and three ligand-binding sites have been located. Two, of these form the active site and bind the substrates F6P and ATP. The, third site binds both allosteric activator and inhibitor. The complex of, the enzyme with F6P and ADP has been partly refined at 2.4 A resolution, and a model of ATP has been built into the active site by using the, refined model of ADP and a 6 A resolution map of bound, 5'-adenylylimidodiphosphate (AMPPNP). The gamma-phosphate of ATP is close, to the 1-hydroxyl of F6P, in a suitable position for in-line phosphoryl, transfer. The binding of the phosphate of F6P involves two arginines from, a neighbouring subunit in the tetramer, which suggests that a, rearrangement of the subunits could explain the cooperativity of substrate, binding. The activatory ADP is also bound by residues from two subunits.
+Phosphofructokinase from Bacillus stearothermophilus shows cooperative kinetics with respect to the substrate fructose-6-phosphate (F6P), allosteric activation by ADP, and inhibition by phosphoenolpyruvate. The crystal structure of the active conformation of the enzyme has been solved to 2.4 A resolution, and three ligand-binding sites have been located. Two of these form the active site and bind the substrates F6P and ATP. The third site binds both allosteric activator and inhibitor. The complex of the enzyme with F6P and ADP has been partly refined at 2.4 A resolution, and a model of ATP has been built into the active site by using the refined model of ADP and a 6 A resolution map of bound 5'-adenylylimidodiphosphate (AMPPNP). The gamma-phosphate of ATP is close to the 1-hydroxyl of F6P, in a suitable position for in-line phosphoryl transfer. The binding of the phosphate of F6P involves two arginines from a neighbouring subunit in the tetramer, which suggests that a rearrangement of the subunits could explain the cooperativity of substrate binding. The activatory ADP is also bound by residues from two subunits.
 ==About this Structure==
-PFK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=3PFK OCA].
+PFK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PFK OCA].
 ==Reference==
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 [[Category: Geobacillus stearothermophilus]]
 [[Category: Single protein]]
-[[Category: Evans, P.R.]]
+[[Category: Evans, P R.]]
-[[Category: Hudson, P.J.]]
+[[Category: Hudson, P J.]]
 [[Category: PO4]]
 [[Category: transferase(phosphotransferase)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:55:32 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:10:46 2008''