Dynamics of Ligand Binding to a Rigid Glycosidase**

Fredj Ben Bdira; Christopher A Waudby; Alexander N Volkov; Sybrin P Schröder; Eiso Ab; Jeroen D C Codée; Hermen S Overkleeft; Johannes M F G Aerts; Hugo van Ingen; Marcellus Ubbink

doi:10.1002/anie.202003236

Dynamics of Ligand Binding to a Rigid Glycosidase**

Fredj Ben Bdira, Christopher A Waudby, Alexander N Volkov, Sybrin P Schröder, Eiso Ab, Jeroen D C Codée, Hermen S Overkleeft, Johannes M F G Aerts, Hugo van Ingen, Marcellus Ubbink

Research output: Contribution to journal › Article › Academic › peer-review

Abstract

The single-domain GH11 glycosidase from Bacillus circulans (BCX) is involved in the degradation of hemicellulose, which is 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, which is 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.

Original language	English
Pages (from-to)	20508-20514
Number of pages	7
Journal	Angewandte Chemie-International Edition
Volume	59
Issue number	46
DOIs	https://doi.org/10.1002/anie.202003236
Publication status	Published - 9 Nov 2020
Externally published	Yes

Keywords

dynamics
glycosidases
ligand binding
NMR spectroscopy
rigid fold

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10.1002/anie.202003236

anie.202003236Final published version, 1.88 MB

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title = "Dynamics of Ligand Binding to a Rigid Glycosidase**",

abstract = "The single-domain GH11 glycosidase from Bacillus circulans (BCX) is involved in the degradation of hemicellulose, which is 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, which is 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.",

keywords = "dynamics, glycosidases, ligand binding, NMR spectroscopy, rigid fold",

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doi = "10.1002/anie.202003236",

language = "English",

volume = "59",

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journal = "Angewandte Chemie-International Edition",

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T1 - Dynamics of Ligand Binding to a Rigid Glycosidase**

AU - Ben Bdira, Fredj

AU - Waudby, Christopher A

AU - Volkov, Alexander N

AU - Schröder, Sybrin P

AU - Ab, Eiso

AU - Codée, Jeroen D C

AU - Overkleeft, Hermen S

AU - Aerts, Johannes M F G

AU - van Ingen, Hugo

AU - Ubbink, Marcellus

PY - 2020/11/9

Y1 - 2020/11/9

N2 - The single-domain GH11 glycosidase from Bacillus circulans (BCX) is involved in the degradation of hemicellulose, which is 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, which is 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.

AB - The single-domain GH11 glycosidase from Bacillus circulans (BCX) is involved in the degradation of hemicellulose, which is 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, which is 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.

KW - dynamics

KW - glycosidases

KW - ligand binding

KW - NMR spectroscopy

KW - rigid fold

U2 - 10.1002/anie.202003236

DO - 10.1002/anie.202003236

M3 - Article

C2 - 32533782

SN - 1433-7851

VL - 59

SP - 20508

EP - 20514

JO - Angewandte Chemie-International Edition

JF - Angewandte Chemie-International Edition

IS - 46

ER -

Dynamics of Ligand Binding to a Rigid Glycosidase**

Abstract

Keywords

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