Structural highlights
Publication Abstract from PubMed
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.
Neutron Crystallographic Studies Reveal Hydrogen Bond and Water-Mediated Interactions between a Carbohydrate-Binding Module and Its Bound Carbohydrate Ligand.,Fisher SZ, von Schantz L, Hakansson M, Logan DT, Ohlin M Biochemistry. 2015 Oct 27;54(42):6435-8. doi: 10.1021/acs.biochem.5b01058. Epub, 2015 Oct 13. PMID:26451738[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Fisher SZ, von Schantz L, Hakansson M, Logan DT, Ohlin M. Neutron Crystallographic Studies Reveal Hydrogen Bond and Water-Mediated Interactions between a Carbohydrate-Binding Module and Its Bound Carbohydrate Ligand. Biochemistry. 2015 Oct 27;54(42):6435-8. doi: 10.1021/acs.biochem.5b01058. Epub, 2015 Oct 13. PMID:26451738 doi:http://dx.doi.org/10.1021/acs.biochem.5b01058
