Ubbink, M;
Ben Bdira, F;
Waudby, CA;
Volkov, AN;
Schröder, SP;
Ab, E;
Codée, JDC;
... van Ingen, H; + view all
(2020)
Dynamics of ligand binding to a rigid glycosidase.
Angewandte Chemie International Edition
10.1002/anie.202003236.
(In press).
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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.
Type: | Article |
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Title: | Dynamics of ligand binding to a rigid glycosidase |
Location: | Germany |
Open access status: | An open access version is available from UCL Discovery |
DOI: | 10.1002/anie.202003236 |
Publisher version: | http://dx.doi.org/10.1002/anie.202003236 |
Language: | English |
Additional information: | 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/ |
Keywords: | Glycosidases, NMR spectroscopy, dynamics, ligand binding, rigid fold |
UCL classification: | UCL UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Structural and Molecular Biology |
URI: | https://discovery.ucl.ac.uk/id/eprint/10107681 |




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