Structure of the starch-debranching enzyme barley limit dextrinase reveals homology of the N-terminal domain to CBM21

Publication: Research - peer-reviewJournal article – Annual report year: 2012

Standard

Harvard

APA

CBE

MLA

Vancouver

Author

Bibtex

@article{34f4d90a7d6343ef9b71052ddf8cbe15,
title = "Structure of the starch-debranching enzyme barley limit dextrinase reveals homology of the N-terminal domain to CBM21",
publisher = "Wiley-Blackwell Publishing, Inc.",
author = "Møller, {Marie Sofie} and {Abou Hachem}, Maher and Birte Svensson and Anette Henriksen",
year = "2012",
doi = "10.1107/S1744309112031004",
volume = "68",
number = "Pt 9",
pages = "1008--1012",
journal = "Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online",
issn = "1744-3091",

}

RIS

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 Publishing, Inc.

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 -