Structure of the starch-debranching enzyme barley limit dextrinase reveals homology of the N-terminal domain to CBM21
Publication: Research - peer-review › Journal article – Annual report year: 2012
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Structure of the starch-debranching enzyme barley limit dextrinase reveals homology of the N-terminal domain to CBM21. / Møller, Marie Sofie; Abou Hachem, Maher ; Svensson, Birte; Henriksen, Anette.
In: Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online, Vol. 68, No. Pt 9, 2012, p. 1008-1012.Publication: Research - peer-review › Journal article – Annual report year: 2012
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TY - JOUR
T1 - Structure of the starch-debranching enzyme barley limit dextrinase reveals homology of the N-terminal domain to CBM21
A1 - Møller,Marie Sofie
A1 - Abou Hachem,Maher
A1 - Svensson,Birte
A1 - Henriksen,Anette
AU - Møller,Marie Sofie
AU - Abou Hachem,Maher
AU - Svensson,Birte
AU - Henriksen,Anette
PB - Wiley-Blackwell Munksgaard
PY - 2012
Y1 - 2012
N2 - 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.
AB - 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.
U2 - 10.1107/S1744309112031004
DO - 10.1107/S1744309112031004
JO - Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online
JF - Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online
SN - 1744-3091
IS - Pt 9
VL - 68
SP - 1008
EP - 1012
ER -