Neutron Crystallographic Studies Reveal Hydrogen Bond and Water-Mediated Interactions between a Carbohydrate-Binding Module and Its Bound Carbohydrate Ligand.
Fisher, Zoe LU ; von Schantz, Laura LU ; Håkansson, Maria LU ; Logan, Derek LU
and
Ohlin, Mats
LU
(2015)
In Biochemistry
54(42).
p.6435-6438
- 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.
Please use this url to cite or link to this publication:
http://lup.lub.lu.se/record/8155614
- author
-
Fisher, Zoe
LU
;
von Schantz, Laura
LU
;
Håkansson, Maria
LU
;
Logan, Derek
LU
and
Ohlin, Mats
LU
- organization
- publishing date
- 2015
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Biochemistry
- volume
- 54
- issue
- 42
- pages
- 6435 - 6438
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- pmid:26451738
- wos:000363916200001
- scopus:84945567452
- pmid:26451738
- ISSN
- 0006-2960
- DOI
- 10.1021/acs.biochem.5b01058
- project
- Designed carbohydrate binding modules and molecular probes
- language
- English
- LU publication?
- yes
- id
- b21ac34a-acc3-4ec1-a053-fdfcaa73cf4d (old id 8155614)
- date added to LUP
- 2016-04-01 10:32:14
- date last changed
- 2020-04-07 01:23:12
@article{b21ac34a-acc3-4ec1-a053-fdfcaa73cf4d,
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 = {Fisher, Zoe and von Schantz, Laura and Håkansson, Maria and Logan, Derek and Ohlin, Mats},
issn = {0006-2960},
language = {eng},
number = {42},
pages = {6435--6438},
publisher = {The American Chemical Society (ACS)},
series = {Biochemistry},
title = {Neutron Crystallographic Studies Reveal Hydrogen Bond and Water-Mediated Interactions between a Carbohydrate-Binding Module and Its Bound Carbohydrate Ligand.},
url = {http://dx.doi.org/10.1021/acs.biochem.5b01058},
doi = {10.1021/acs.biochem.5b01058},
volume = {54},
year = {2015},
}