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@ARTICLE{Banaszak:95857,
      author       = {Banaszak, K. and Mechin, I. and Obmolova, G. and Oldham, M.
                      and Chang, S. H. and Ruiz, T. and Radermacher, M. and
                      Kopperschlaeger, G. and Rypniewski, W. and DESY},
      title        = {{T}he crystal structures of eukaryotic phosphofructokinases
                      from baker's yeast and rabbit skeletal muscle.},
      journal      = {Journal of molecular biology},
      volume       = {407},
      issn         = {0022-2836},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {PHPPUBDB-19271},
      pages        = {284-297},
      year         = {2011},
      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.},
      keywords     = {Animals / Binding Sites: genetics / Crystallography /
                      Eukaryota: enzymology / Fructosephosphates: metabolism /
                      Glycolysis: genetics / Models, Molecular / Muscle, Skeletal:
                      enzymology / Phosphofructokinase-1: chemistry /
                      Phosphofructokinase-1: genetics / Phosphofructokinase-1:
                      metabolism / Phosphofructokinases: chemistry /
                      Phosphofructokinases: genetics / Phosphofructokinases:
                      metabolism / Rabbits / Saccharomyces cerevisiae: enzymology
                      / Saccharomyces cerevisiae: genetics / Fructosephosphates
                      (NLM Chemicals) / fructose-6-phosphate (NLM Chemicals) /
                      Phosphofructokinases (NLM Chemicals) / Phosphofructokinase-1
                      (NLM Chemicals)},
      cin          = {EMBL},
      ddc          = {570},
      cid          = {$I:(DE-H253)EMBL_-2012_-20130307$},
      pnm          = {DORIS Beamline BW7 (POF2-54G13)},
      pid          = {G:(DE-H253)POF2-BW7-20130405},
      experiment   = {EXP:(DE-H253)D-BW7-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:21241708},
      UT           = {WOS:000288925100007},
      doi          = {10.1016/j.jmb.2011.01.019},
      url          = {https://bib-pubdb1.desy.de/record/95857},
}