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Dynamics of Ligand Binding to a Rigid Glycosidase

Ben Bdira, F; Waudby, CA; Volkov, AN; Schröder, SP; AB, E; Codée, JDC; Overkleeft, HS; ... Ubbink, M; + view all (2020) Dynamics of Ligand Binding to a Rigid Glycosidase. Angewandte Chemie 10.1002/ange.202003236. Green open access

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Abstract

The enzyme xylanase from Bacillus circulans (BCX) is involved in the breakdown of xylan, which is one of the most abundant materials in wood. NMR experiments demonstrate that in solution the enzyme is rigid and does not change its structure during turnover. Binding of the substrate occurs in many orientations, including a distorted form. A model is presented for the effect of substrate dynamics on enzyme function.

Type: Article
Title: Dynamics of Ligand Binding to a Rigid Glycosidase
Open access status: An open access version is available from UCL Discovery
DOI: 10.1002/ange.202003236
Publisher version: https://doi.org/10.1002/ange.202003236
Language: English
Additional information: This is an open access article under the terms of the Creative Commons Attribution‐NonCommercial‐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.
Keywords: dynamics, glycosidases, ligand binding, NMR spectroscopy, rigid fold
UCL classification: UCL
UCL > Provost and Vice Provost Offices
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/10109530
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