PDBsum entry 3o8o

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protein ligands Protein-protein interface(s) links
Transferase PDB id
Protein chains
750 a.a. *
763 a.a. *
F6P ×8
FDP ×8
* Residue conservation analysis
PDB id:
Name: Transferase
Title: Structure of phosphofructokinase from saccharomyces cerevisi
Structure: 6-phosphofructokinase subunit alpha. Chain: a, c, e, g. Synonym: phosphofructokinase 1, phosphohexokinase, 6pf-1-k alpha. Engineered: yes. 6-phosphofructokinase subunit beta. Chain: b, d, f, h. Synonym: phosphofructokinase 2, phosphohexokinase, 6pf-1-k beta.
Source: Saccharomyces cerevisiae. Brewer's yeast,lager beer yeast,yeast. Organism_taxid: 4932. Gene: pfk1, ygr240c, g8599. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932. Gene: pfk2, ymr205c, ym8325.06c.
2.90Å     R-factor:   0.259     R-free:   0.309
Authors: K.Banaszak,I.Mechin,G.Kopperschlager,W.Rypniewski
Key ref: K.Banaszak et al. (2011). The crystal structures of eukaryotic phosphofructokinases from baker's yeast and rabbit skeletal muscle. J Mol Biol, 407, 284-297. PubMed id: 21241708 DOI: 10.1016/j.jmb.2011.01.019
03-Aug-10     Release date:   02-Feb-11    
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Protein chains
Pfam   ArchSchema ?
P16861  (K6PF1_YEAST) -  ATP-dependent 6-phosphofructokinase subunit alpha
987 a.a.
750 a.a.
Protein chains
Pfam   ArchSchema ?
P16862  (K6PF2_YEAST) -  ATP-dependent 6-phosphofructokinase subunit beta
959 a.a.
763 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     fructose 6-phosphate metabolic process   2 terms 
  Biochemical function     ATP binding     2 terms  


DOI no: 10.1016/j.jmb.2011.01.019 J Mol Biol 407:284-297 (2011)
PubMed id: 21241708  
The crystal structures of eukaryotic phosphofructokinases from baker's yeast and rabbit skeletal muscle.
K.Banaszak, I.Mechin, G.Obmolova, M.Oldham, S.H.Chang, T.Ruiz, M.Radermacher, G.Kopperschläger, W.Rypniewski.
Phosphofructokinase 1 (PFK) is a multisubunit allosteric enzyme that catalyzes the principal regulatory step in glycolysis-the phosphorylation of fructose 6-phosphate to fructose 1,6-bisphosphate by ATP. The activity of eukaryotic PFK is modulated by a number of effectors in response to the cell's needs for energy and building blocks for biosynthesis. The crystal structures of eukaryotic PFKs-from Saccharomyces cerevisiae and rabbit skeletal muscle-demonstrate how successive gene duplications and fusion are reflected in the protein structure and how they allowed the evolution of new functionalities. The basic framework inherited from prokaryotes is conserved, and additional levels of structural and functional complexity have evolved around it. Analysis of protein-ligand complexes has shown how PFK is activated by fructose 2,6-bisphosphate (a powerful PFK effector found only in eukaryotes) and reveals a novel nucleotide binding site. Crystallographic results have been used as the basis for structure-based effector design.

Literature references that cite this PDB file's key reference

  PubMed id Reference
23149688 A.P.Oliveira, C.Ludwig, P.Picotti, M.Kogadeeva, R.Aebersold, and U.Sauer (2012).
Regulation of yeast central metabolism by enzyme phosphorylation.
  Mol Syst Biol, 8, 623.  
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