3pfk: Difference between revisions
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|PDB= 3pfk |SIZE=350|CAPTION= <scene name='initialview01'>3pfk</scene>, resolution 2.4Å | |PDB= 3pfk |SIZE=350|CAPTION= <scene name='initialview01'>3pfk</scene>, resolution 2.4Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene> | |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] | |ACTIVITY= <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> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3pfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pfk OCA], [http://www.ebi.ac.uk/pdbsum/3pfk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3pfk RCSB]</span> | |||
}} | }} | ||
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[[Category: Evans, P R.]] | [[Category: Evans, P R.]] | ||
[[Category: Hudson, P J.]] | [[Category: Hudson, P J.]] | ||
[[Category: transferase(phosphotransferase)]] | [[Category: transferase(phosphotransferase)]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:35:20 2008'' | ||
Revision as of 05:35, 31 March 2008
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| , resolution 2.4Å | |||||||
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| Ligands: | |||||||
| Activity: | 6-phosphofructokinase, with EC number 2.7.1.11 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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