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

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.

• Författare: Zoe Fisher; Laura von Schantz; Maria Håkansson; Derek Logan; Mats Ohlin
• Avdelning/ar: European Spallation Source ESS AB; Institutionen för immunteknologi; Biokemi och Strukturbiologi
• Publiceringsår: 2015
• Språk: Engelska
• Sidor: 6435-6438
• Publikation/Tidskrift/Serie: Biochemistry
• Volym: 54
• Issue: 42
• Länkar: http://dx.doi.org/10.1021/acs.biochem.5b01058
• Dokumenttyp: Artikel i tidskrift
• Förlag: The American Chemical Society (ACS)
• Ämne: Biochemistry and Molecular Biology
• Status: Published
• Projekt: Designed carbohydrate binding modules and molecular probes
• ISBN/ISSN/Övrigt: ISSN: 0006-2960