3pfk: Difference between revisions
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[[Image:3pfk.gif|left|200px]] | [[Image:3pfk.gif|left|200px]] | ||
'''PHOSPHOFRUCTOKINASE. STRUCTURE AND CONTROL''' | {{Structure | ||
|PDB= 3pfk |SIZE=350|CAPTION= <scene name='initialview01'>3pfk</scene>, resolution 2.4Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene> | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''PHOSPHOFRUCTOKINASE. STRUCTURE AND CONTROL''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
3PFK is a [ | 3PFK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PFK OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/6115424 6115424] | ||
[[Category: 6-phosphofructokinase]] | [[Category: 6-phosphofructokinase]] | ||
[[Category: Geobacillus stearothermophilus]] | [[Category: Geobacillus stearothermophilus]] | ||
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[[Category: transferase(phosphotransferase)]] | [[Category: transferase(phosphotransferase)]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:06:32 2008'' | ||
Revision as of 20:06, 20 March 2008
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| , resolution 2.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | 6-phosphofructokinase, with EC number 2.7.1.11 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
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