Journal article
Structure of the starch-debranching enzyme barley limit dextrinase reveals homology of the N-terminal domain to CBM21
Barley limit dextrinase (HvLD) is a debranching enzyme from glycoside hydrolase family 13 subfamily 13 (GH13_13) that hydrolyses α-1,6-glucosidic linkages in limit dextrins derived from amylopectin. The structure of HvLD was solved and refined to 1.9 Å resolution. The structure has a glycerol molecule in the active site and is virtually identical to the structures of HvLD in complex with the competitive inhibitors α-cyclodextrin and β-cyclodextrin solved to 2.5 and 2.1 Å resolution, respectively.
However, three loops in the N-terminal domain that are shown here to resemble carbohydrate-binding module family 21 were traceable and were included in the present HvLD structure but were too flexible to be traced and included in the structures of the two HvLD-inhibitor complexes.
Language: | English |
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Publisher: | International Union of Crystallography |
Year: | 2012 |
Pages: | 1008-1012 |
ISSN: | 17443091 and 2053230x |
Types: | Journal article |
DOI: | 10.1107/S1744309112031004 |
ORCIDs: | Møller, Marie Sofie , Abou Hachem, Maher and Svensson, Birte |