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@ARTICLE{Matrai:85680,
      author       = {Matrai, J. and Lammens, W. and Jonckheer, A. and Le Roy, K.
                      and Rabijns, A. and Van den Ende, W. and De Maeyer, M. and
                      DESY},
      title        = {{A}n alternate sucrose binding mode in the {E}203{Q}
                      {A}rabidopsis invertase mutant: {A}n {X}-ray crystallography
                      and docking study},
      journal      = {Proteins},
      volume       = {71},
      issn         = {0887-3585},
      address      = {New York, NY},
      publisher    = {Wiley-Liss},
      reportid     = {PHPPUBDB-8387},
      pages        = {552-564},
      year         = {2008},
      abstract     = {In the present study, we report on the X-ray
                      crystallographic structure of a GH32 invertase mutant,
                      (i.e., the Arabidopsis thaliana cell-wall invertase 1-E203Q,
                      AtcwINV1-mutant) in complex with sucrose. This structure was
                      solved to reveal the features of sugar binding in the
                      catalytic pocket. However, as demonstrated by the X-ray
                      structure the sugar binding and the catalytic pocket
                      arrangement is significantly altered as compared with what
                      was expected based on previous X-ray structures on GH-J clan
                      enzymes. We performed a series of docking and molecular
                      dynamics simulations on various derivatives of AtcwINV1 to
                      reveal the reasons behind this modified sugar binding. Our
                      results demonstrate that the E203Q mutation introduced into
                      the catalytic pocket triggers conformational changes that
                      alter the wild type substrate binding. In addition, this
                      study also reveals the putative productive sucrose binding
                      modus in the wild type enzyme.},
      keywords     = {Amino Acid Substitution / Arabidopsis: enzymology /
                      Computer Simulation / Crystallization / Crystallography,
                      X-Ray / Models, Molecular / Protein Conformation: drug
                      effects / Sucrose: metabolism / beta-Fructofuranosidase:
                      chemistry / beta-Fructofuranosidase: genetics /
                      beta-Fructofuranosidase: metabolism / Sucrose (NLM
                      Chemicals) / beta-Fructofuranosidase (NLM Chemicals)},
      cin          = {EMBL},
      ddc          = {540},
      cid          = {$I:(DE-H253)EMBL_-2012_-20130307$},
      pnm          = {FS Beamline without reference (POF1-550)},
      pid          = {G:(DE-H253)POF1-No-Ref-20130405},
      experiment   = {EXP:(DE-H253)Unknown-BL-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:17963237},
      UT           = {WOS:000254263400005},
      doi          = {10.1002/prot.21700},
      url          = {https://bib-pubdb1.desy.de/record/85680},
}