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

doi:10.1021/acs.biochem.5b01058

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

SARomics Biostructures AB

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

Abstract

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.

Original language	English
Pages (from-to)	6435-6438
Journal	Biochemistry
Volume	54
Issue number	42
DOIs	https://doi.org/10.1021/acs.biochem.5b01058
Publication status	Published - 2015

Subject classification (UKÄ)

Biochemistry and Molecular Biology

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10.1021/acs.biochem.5b01058

Designed carbohydrate binding modules and molecular probes
Ohlin, M. (PI), Cicortas Gunnarsson, L. (Research student), von Schantz, L. (Research student), Holst, O. (Assistant supervisor), Nordberg Karlsson, E. (Assistant supervisor) & Logan, D. (Researcher)
Swedish Research Council
2001/01/01 → 2015/12/31
Project: Research

Cite this

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

abstract = "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.",

author = "Zoe Fisher and {von Schantz}, Laura and Maria H{\aa}kansson and Derek Logan and Mats Ohlin",

year = "2015",

doi = "10.1021/acs.biochem.5b01058",

language = "English",

volume = "54",

pages = "6435--6438",

journal = "Biochemistry",

issn = "0006-2960",

publisher = "The American Chemical Society (ACS)",

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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

C2 - 26451738

SN - 0006-2960

VL - 54

SP - 6435

EP - 6438

JO - Biochemistry

JF - Biochemistry

IS - 42

ER -

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

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Subject classification (UKÄ)

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Designed carbohydrate binding modules and molecular probes

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