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

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Neutron Crystallographic Studies Reveal Hydrogen Bond and Water-Mediated Interactions between a Carbohydrate-Binding Module and Its Bound Carbohydrate Ligand. / Fisher, Zoe; von Schantz, Laura; Håkansson, Maria; Logan, Derek; Ohlin, Mats.

In: Biochemistry, Vol. 54, No. 42, 2015, p. 6435-6438.

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T1 - Neutron Crystallographic Studies Reveal Hydrogen Bond and Water-Mediated Interactions between a Carbohydrate-Binding Module and Its Bound Carbohydrate Ligand.

AU - Fisher, Zoe

AU - von Schantz, Laura

AU - Håkansson, Maria

AU - Logan, Derek

AU - Ohlin, Mats

PY - 2015

Y1 - 2015

N2 - 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.

AB - 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.

U2 - 10.1021/acs.biochem.5b01058

DO - 10.1021/acs.biochem.5b01058

M3 - Article

VL - 54

SP - 6435

EP - 6438

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 42

ER -