4R27

Crystal structure of beta-glycosidase BGL167

Summary for 4R27

• Entry DOI: 10.2210/pdb4r27/pdb
• Descriptor: Glycoside hydrolase (2 entities in total)
• Functional Keywords: glycoside hydrolase, hydrolase
• Biological source: Microbacterium sp. Gsoil167
• Total number of polymer chains: 2
• Total formula weight: 95612.56

Authors

Park, S.J.,Choi, J.M.,Kyeong, H.H.,Kim, S.G.,Kim, H.S. (deposition date: 2014-08-09, release date: 2015-05-27, Last modification date: 2023-11-08)

Primary citation

Park, S.J.,Choi, J.M.,Kyeong, H.H.,Kim, S.G.,Kim, H.S.
Rational design of a beta-glycosidase with high regiospecificity for triterpenoid tailoring
Chembiochem, 16:854-860, 2015

PubMed Abstract: Triterpenoids with desired glycosylation patterns have attracted considerable attention as potential therapeutics for inflammatory diseases and various types of cancer. Sugar-hydrolyzing enzymes with high substrate specificity would be far more efficient than other methods for the synthesis of such specialty triterpenoids, but they are yet to be developed. Here we present a strategy to rationally design a β-glycosidase with high regiospecificity for triterpenoids. A β-glycosidase with broad substrate specificity was isolated, and its crystal structure was determined at 2.0 Å resolution. Based on the product profiles and substrate docking simulations, we modeled the substrate binding modes of the enzyme. From the model, the substrate binding cleft of the enzyme was redesigned in a manner that preferentially hydrolyzes glycans at specific glycosylation sites of triterpenoids. The designed mutants were shown to produce a variety of specialty triterpenoids with high purity.

PubMed: 25703680
DOI: 10.1002/cbic.201500004

Experimental method

X-RAY DIFFRACTION (2.03 Å)