spacer
spacer

PDBsum entry 3o8o

Go to PDB code: 
protein ligands Protein-protein interface(s) links
Transferase PDB id
3o8o
Jmol
Contents
Protein chains
750 a.a. *
763 a.a. *
Ligands
F6P ×8
FDP ×8
* Residue conservation analysis
PDB id:
3o8o
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.
Resolution:
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
Date:
03-Aug-10     Release date:   02-Feb-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P16861  (K6PF1_YEAST) -  ATP-dependent 6-phosphofructokinase subunit alpha
Seq:
Struc:
 
Seq:
Struc:
987 a.a.
750 a.a.
Protein chains
Pfam   ArchSchema ?
P16862  (K6PF2_YEAST) -  ATP-dependent 6-phosphofructokinase subunit beta
Seq:
Struc:
 
Seq:
Struc:
959 a.a.
763 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains A, B, C, D, E, F, G, H: 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
+ 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   1 term 
  Biological process     fructose 6-phosphate metabolic process   2 terms 
  Biochemical function     ATP binding     2 terms  

 

 
    reference    
 
 
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.
 
  ABSTRACT  
 
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.  
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.