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Neutron Crystallographic Studies Reveal Hydrogen Bond and Water-Mediated Interactions between a Carbohydrate-Binding Module and Its Bound Carbohydrate Ligand.

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Author

Summary, in English

Carbohydrate-binding modules (CBMs) are key components of many carbohydrate-modifying enzymes. CBMs affect the activity of these enzymes by modulating bonding and catalysis. To further characterize and study CBM-ligand binding interactions, neutron crystallographic studies of an engineered family 4-type CBM in complex with a branched xyloglucan ligand were conducted. The first neutron crystal structure of a CBM-ligand complex reported here shows numerous atomic details of hydrogen bonding and water-mediated interactions and reveals the charged state of key binding cleft amino acid side chains.

Publishing year

2015

Language

English

Pages

6435-6438

Publication/Series

Biochemistry

Volume

54

Issue

42

Document type

Journal article

Publisher

The American Chemical Society (ACS)

Topic

  • Biochemistry and Molecular Biology

Status

Published

Project

  • Designed carbohydrate binding modules and molecular probes

ISBN/ISSN/Other

  • ISSN: 0006-2960