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@ARTICLE{Li:859977,
      author       = {Li, Zhihong and Zhang, Xiaoshuai and Wang, Qingqing and Li,
                      Chunran and Zhang, Nianying and Zhang, Xinkai and Xu, Birui
                      and Ma, Baoliang and Schrader, Tobias E. and Coates,
                      Leighton and Kovalevsky, Andrey and Huang, Yandong and Wan,
                      Qun},
      title        = {{U}nderstanding the p{H}-{D}ependent {R}eaction {M}echanism
                      of a {G}lycoside {H}ydrolase {U}sing {H}igh-{R}esolution
                      {X}-ray and {N}eutron {C}rystallographyülcih},
      journal      = {ACS catalysis},
      volume       = {8},
      number       = {9},
      issn         = {2155-5435},
      address      = {Washington, DC},
      publisher    = {ACS},
      reportid     = {FZJ-2019-00783},
      pages        = {8058 - 8069},
      year         = {2018},
      abstract     = {Glycoside hydrolases (GHs) commonly use the retaining or
                      inverting mechanisms to hydrolyze carbohydrates, and the
                      rates of catalysis are usually pH dependent. Deeper
                      understanding of these pH-dependent reaction mechanisms is
                      of great importance for protein engineering and drug design.
                      We used high-resolution X-ray crystallography to analyze the
                      sugar ring configurations of an oligosaccharide ligand
                      during hydrolysis for the family 11 GH, and the results
                      support the 1S3 → 4H3 → 4C1 conformational itinerary.
                      These results indicate that sugar ring flexibility may help
                      to distort and break the glycosidic bond. Constant pH
                      molecular dynamics simulations and neutron crystallography
                      demonstrate that the catalytic glutamate residue (E177) has
                      alternate conformational changes to transfer a proton to
                      cleave the glycosidic bond. Furthermore, a neutron
                      crystallography analysis shows that the H-bond length
                      between E177 and its nearby tyrosine residue (Y88) is
                      shortened when the pH increases, preventing E177 from
                      rotating downward and obtaining a proton from the solvent
                      for catalysis. This result indicates that the H-bond length
                      variation may play a key role in the pH-dependent reaction
                      mechanism. In summary, our results demonstrate that both
                      sugar ring flexibility and protein dynamics are important in
                      the pH-dependent reaction mechanism and may help to engineer
                      GHs with different pH optima.},
      cin          = {JCNS-FRM-II / JCNS-1},
      ddc          = {540},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106},
      pnm          = {6G15 - FRM II / MLZ (POF3-6G15) / 6G4 - Jülich Centre for
                      Neutron Research (JCNS) (POF3-623) / 6215 - Soft Matter,
                      Health and Life Sciences (POF3-621)},
      pid          = {G:(DE-HGF)POF3-6G15 / G:(DE-HGF)POF3-6G4 /
                      G:(DE-HGF)POF3-6215},
      experiment   = {EXP:(DE-MLZ)BIODIFF-20140101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000444364800034},
      doi          = {10.1021/acscatal.8b01472},
      url          = {https://juser.fz-juelich.de/record/859977},
}