@article{discovery10107681,
         journal = {Angewandte Chemie International Edition},
            note = {This is an
open access article under the terms of the Creative Commons
Attribution Non-Commercial NoDerivs License, which permits use
and distribution in any medium, provided the original work is
properly cited, the use is non-commercial, and no modifications or
adaptations are made. See here for more information: https://creativecommons.org/licenses/by-nc-nd/4.0/},
           title = {Dynamics of ligand binding to a rigid glycosidase},
            year = {2020},
           month = {September},
        keywords = {Glycosidases, NMR spectroscopy, dynamics, ligand binding, rigid fold},
             url = {http://dx.doi.org/10.1002/anie.202003236},
          author = {Ubbink, M and Ben Bdira, F and Waudby, CA and Volkov, AN and Schr{\"o}der, SP and Ab, E and Cod{\'e}e, JDC and Overkleeft, HS and Aerts, HMFG and van Ingen, H},
        abstract = {The single-domain GH11 glycosidase from� Bacillus circulans �(BCX) is involved in the degradation of hemicellulose, one of the most abundant renewable biomaterials in nature. We demonstrate that BCX in solution undergoes minimal structural changes during turnover. NMR spectroscopy results show that the rigid protein matrix provides a frame for fast substrate binding in multiple conformations, accompanied by slow conversion, attributed to an enzyme induced substrate distortion. A model is proposed in which the rigid enzyme takes advantage of substrate flexibility to induce a conformation that facilitates the acyl formation step of the hydrolysis reaction.}
}