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

Zoe Fisher, Laura von Schantz, Maria Håkansson, Derek Logan, Mats Ohlin

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskriftPeer review

12 Citeringar (SciVal)

Sammanfattning

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.
Originalspråkengelska
Sidor (från-till)6435-6438
TidskriftBiochemistry
Volym54
Utgåva42
DOI
StatusPublished - 2015

Ämnesklassifikation (UKÄ)

  • Biokemi och molekylärbiologi

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