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Transferase(phosphotransferase) PDB id
4pfk
Jmol
Contents
Protein chain
319 a.a. *
Ligands
F6P
ADP ×2
Metals
_MG ×2
Waters ×70
* Residue conservation analysis
PDB id:
4pfk
Name: Transferase(phosphotransferase)
Title: Phosphofructokinase. Structure and control
Structure: Phosphofructokinase. Chain: a. Engineered: yes
Source: Geobacillus stearothermophilus. Organism_taxid: 1422. Cell_line: 293.
Biol. unit: Tetramer (from PQS)
Resolution:
2.40Å     R-factor:   0.169    
Authors: P.R.Evans,P.J.Hudson
Key ref: P.R.Evans et al. (1981). Phosphofructokinase: structure and control. Philos Trans R Soc Lond B Biol Sci, 293, 53-62. PubMed id: 6115424
Date:
25-Jan-88     Release date:   09-Jan-89    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00512  (K6PF_GEOSE) -  6-phosphofructokinase
Seq:
Struc: 		319 a.a.
319 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.2.7.1.11  - 6-phosphofructokinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate
ATP
 +
D-fructose 6-phosphate
Bound ligand (Het Group name = F6P)
corresponds exactly 		=
ADP
Bound ligand (Het Group name = ADP)
corresponds exactly 		+ D-fructose 1,6-bisphosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   2 terms 
  Biological process     metabolic process   4 terms 
  Biochemical function     catalytic activity     8 terms  

 

 
    reference    
 
 
Philos Trans R Soc Lond B Biol Sci 293:53-62 (1981)
PubMed id: 6115424  
 
 
Phosphofructokinase: structure and control.
P.R.Evans, G.W.Farrants, P.J.Hudson.
 
  ABSTRACT  
 
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.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21124851 A.Usenik, and M.LegiĊĦa (2010).
Evolution of allosteric citrate binding sites on 6-phosphofructo-1-kinase.
  PLoS One, 5, e15447.  
  20161986 M.Di Marco, S.Shamsuddin, K.A.Razak, A.A.Aziz, C.Devaux, E.Borghi, L.Levy, and C.Sadun (2010).
Overview of the main methods used to combine proteins with nanosystems: absorption, bioconjugation, and encapsulation.
  Int J Nanomedicine, 5, 37-49.  
19553681 M.A.Currie, F.Merino, T.Skarina, A.H.Wong, A.Singer, G.Brown, A.Savchenko, A.Caniuguir, V.Guixé, A.F.Yakunin, and Z.Jia (2009).
ADP-dependent 6-phosphofructokinase from Pyrococcus horikoshii OT3: structure determination and biochemical characterization of PH1645.
  J Biol Chem, 284, 22664-22671.  
18562308 J.Postmus, A.B.Canelas, J.Bouwman, B.M.Bakker, W.van Gulik, M.J.de Mattos, S.Brul, and G.J.Smits (2008).
Quantitative Analysis of the High Temperature-induced Glycolytic Flux Increase in Saccharomyces cerevisiae Reveals Dominant Metabolic Regulation.
  J Biol Chem, 283, 23524-23532.  
17522059 K.Tanneberger, J.Kirchberger, J.Bär, W.Schellenberger, S.Rothemund, M.Kamprad, H.Otto, T.Schöneberg, and A.Edelmann (2007).
A novel form of 6-phosphofructokinase. Identification and functional relevance of a third type of subunit in Pichia pastoris.
  J Biol Chem, 282, 23687-23697.  
  7708014 E.M.Phizicky, and S.Fields (1995).
Protein-protein interactions: methods for detection and analysis.
  Microbiol Rev, 59, 94.  
  7825568 N.Raben, R.Exelbert, R.Spiegel, J.B.Sherman, H.Nakajima, P.Plotz, and J.Heinisch (1995).
Functional expression of human mutant phosphofructokinase in yeast: genetic defects in French Canadian and Swiss patients with phosphofructokinase deficiency.
  Am J Hum Genet, 56, 131-141.  
7876126 W.M.Byrnes, W.Hu, E.S.Younathan, and S.H.Chang (1995).
A chimeric bacterial phosphofructokinase exhibits cooperativity in the absence of heterotropic regulation.
  J Biol Chem, 270, 3828-3835.  
8202475 I.Auzat, G.Le Bras, and J.R.Garel (1994).
The cooperativity and allosteric inhibition of Escherichia coli phosphofructokinase depend on the interaction between threonine-125 and ATP.
  Proc Natl Acad Sci U S A, 91, 5242-5246.  
  8037209 J.B.Sherman, N.Raben, C.Nicastri, Z.Argov, H.Nakajima, E.M.Adams, C.M.Eng, T.M.Cowan, and P.H.Plotz (1994).
Common mutations in the phosphofructokinase-M gene in Ashkenazi Jewish patients with glycogenesis VII--and their population frequency.
  Am J Hum Genet, 55, 305-313.  
  7513946 S.Tsujino, S.Servidei, P.Tonin, S.Shanske, G.Azan, and S.DiMauro (1994).
Identification of three novel mutations in non-Ashkenazi Italian patients with muscle phosphofructokinase deficiency.
  Am J Hum Genet, 54, 812-819.  
  1651234 L.T.Haber, and G.C.Walker (1991).
Altering the conserved nucleotide binding motif in the Salmonella typhimurium MutS mismatch repair protein affects both its ATPase and mismatch binding activities.
  EMBO J, 10, 2707-2715.  
2869483 D.C.Fry, S.A.Kuby, and A.S.Mildvan (1986).
ATP-binding site of adenylate kinase: mechanistic implications of its homology with ras-encoded p21, F1-ATPase, and other nucleotide-binding proteins.
  Proc Natl Acad Sci U S A, 83, 907-911.  
  6329717 J.E.Walker, M.Saraste, M.J.Runswick, and N.J.Gay (1982).
Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold.
  EMBO J, 1, 945-951.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.