%0 Journal Article
%A Ubbink, M
%A Ben Bdira, F
%A Waudby, CA
%A Volkov, AN
%A Schröder, SP
%A Ab, E
%A Codée, JDC
%A Overkleeft, HS
%A Aerts, HMFG
%A van Ingen, H
%D 2020
%F discovery:10107681
%J Angewandte Chemie International Edition
%K Glycosidases, NMR spectroscopy, dynamics, ligand binding, rigid fold
%T Dynamics of ligand binding to a rigid glycosidase
%U https://discovery.ucl.ac.uk/id/eprint/10107681/
%X 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.
%Z 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/