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@ARTICLE{Zerrad:16685,
      author       = {Zerrad, L. and Merli, A. and Schröder, G.F. and Varga, A.
                      and Gráczer, E. and Pernot, P. and Round, A. and Vas, M.
                      and Bowler, M.W.},
      title        = {{A} {S}pring {L}oaded {R}elease {M}echanism {R}egulates
                      {D}omain {M}ovement and {C}atalysis in {P}hosphoglycerate
                      {K}inase.},
      journal      = {The journal of biological chemistry},
      volume       = {286},
      issn         = {0021-9258},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {PreJuSER-16685},
      pages        = {14040 - 14048},
      year         = {2011},
      note         = {This work was supported in part by Hungarian National
                      Research Grant 77978.},
      abstract     = {Phosphoglycerate kinase (PGK) is the enzyme responsible for
                      the first ATP-generating step of glycolysis and has been
                      implicated extensively in oncogenesis and its development.
                      Solution small angle x-ray scattering (SAXS) data, in
                      combination with crystal structures of the enzyme in complex
                      with substrate and product analogues, reveal a new
                      conformation for the resting state of the enzyme and
                      demonstrate the role of substrate binding in the preparation
                      of the enzyme for domain closure. Comparison of the x-ray
                      scattering curves of the enzyme in different states with
                      crystal structures has allowed the complete reaction cycle
                      to be resolved both structurally and temporally. The enzyme
                      appears to spend most of its time in a fully open
                      conformation with short periods of closure and catalysis,
                      thereby allowing the rapid diffusion of substrates and
                      products in and out of the binding sites. Analysis of the
                      open apoenzyme structure, defined through deformable elastic
                      network refinement against the SAXS data, suggests that
                      interactions in a mostly buried hydrophobic region may favor
                      the open conformation. This patch is exposed on domain
                      closure, making the open conformation more thermodynamically
                      stable. Ionic interactions act to maintain the closed
                      conformation to allow catalysis. The short time PGK spends
                      in the closed conformation and its strong tendency to rest
                      in an open conformation imply a spring-loaded release
                      mechanism to regulate domain movement, catalysis, and
                      efficient product release.},
      keywords     = {Adenosine Triphosphate: chemistry / Amino Acid Sequence /
                      Animals / Binding Sites / Biophysics: methods / Catalysis /
                      Crystallography, X-Ray: methods / Humans / Mice / Molecular
                      Sequence Data / Phosphoglycerate Kinase: chemistry / Protein
                      Conformation / Protein Structure, Secondary / Protein
                      Structure, Tertiary / Scattering, Radiation / Sequence
                      Homology, Amino Acid / Thermodynamics / Adenosine
                      Triphosphate (NLM Chemicals) / Phosphoglycerate Kinase (NLM
                      Chemicals) / J (WoSType)},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {Funktion und Dysfunktion des Nervensystems / BioSoft:
                      Makromolekulare Systeme und biologische
                      Informationsverarbeitung},
      pid          = {G:(DE-Juel1)FUEK409 / G:(DE-Juel1)FUEK505},
      shelfmark    = {Biochemistry $\&$ Molecular Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:21349853},
      pmc          = {pmc:PMC3077604},
      UT           = {WOS:000289556200026},
      doi          = {10.1074/jbc.M110.206813},
      url          = {https://juser.fz-juelich.de/record/16685},
}