Neutron Crystallographic Studies Reveal Hydrogen Bond and Water-Mediated Interactions between a Carbohydrate-Binding Module and Its Bound Carbohydrate Ligand.
(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:
https://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
- 2022-04-12 07:18:15
@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}}, }