5dpn | pdb_00005dpn
From Proteopedia
Engineered CBM X-2 L110F in complex with branched carbohydrate XXXG.
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Structural highlights
Publication Abstract from PubMedCarbohydrate-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
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