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@ARTICLE{Kovacic:280743,
      author       = {Kovacic, Filip and Mandrysch, A. and Poojari, C. and
                      Strodel, Birgit and Jaeger, Karl-Erich},
      title        = {{S}tructural features determining thermal adaptation of
                      esterases},
      journal      = {Protein engineering design and selection},
      volume       = {29},
      number       = {2},
      issn         = {0269-2139},
      address      = {Oxford},
      publisher    = {Oxford Univ. Press},
      reportid     = {FZJ-2016-00500},
      pages        = {65-76},
      year         = {2015},
      abstract     = {The adaptation of microorganisms to extreme living
                      temperatures requires the evolution of enzymes with a high
                      catalytic efficiency under these conditions. Such
                      extremophilic enzymes represent valuable tools to study the
                      relationship between protein stability, dynamics and
                      function. Nevertheless, the multiple effects of temperature
                      on the structure and function of enzymes are still poorly
                      understood at the molecular level. Our analysis of four
                      homologous esterases isolated from bacteria living at
                      temperatures ranging from 10°C to 70°C suggested an
                      adaptation route for the modulation of protein thermal
                      properties through the optimization of local flexibility at
                      the protein surface. While the biochemical properties of the
                      recombinant esterases are conserved, their thermal
                      properties have evolved to resemble those of the respective
                      bacterial habitats. Molecular dynamics simulations at
                      temperatures around the optimal temperatures for enzyme
                      catalysis revealed temperature-dependent flexibility of four
                      surface-exposed loops. While the flexibility of some loops
                      increased with raising the temperature and decreased with
                      lowering the temperature, as expected for those loops
                      contributing to the protein stability, other loops showed an
                      increment of flexibility upon lowering and raising the
                      temperature. Preserved flexibility in these regions seems to
                      be important for proper enzyme function. The structural
                      differences of these four loops, distant from the active
                      site, are substantially larger than for the overall protein
                      structure, indicating that amino acid exchanges within these
                      loops occurred more frequently thereby allowing the bacteria
                      to tune atomic interactions for different temperature
                      requirements without interfering with the overall enzyme
                      function.},
      cin          = {IMET / ICS-6},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IMET-20090612 / I:(DE-Juel1)ICS-6-20110106},
      pnm          = {89581 - Biotechnology (POF2-89581)},
      pid          = {G:(DE-HGF)POF2-89581},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000370301400004},
      pubmed       = {pmid:26647400},
      doi          = {10.1093/protein/gzv061},
      url          = {https://juser.fz-juelich.de/record/280743},
}