Structure of Aspergillus aculeatus β-1,4-galactanase in complex with galactobiose

Søs Torpenholt; Jens-christian N. Poulsen; Sebastian Jannick Muderspach; Leonardo De Maria; Leila Lo Leggio

doi:10.1107/S2053230X19005612

Structure of Aspergillus aculeatus β-1,4-galactanase in complex with galactobiose

Søs Torpenholt, Jens-christian N. Poulsen, Sebastian Jannick Muderspach, Leonardo De Maria, Leila Lo Leggio^*

^*Corresponding author af dette arbejde

1 Citationer (Scopus)

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Abstract

β-1,4-Galactanases are glycoside hydrolases that are involved in the degradation of pectin and belong to family 53 in the classification of glycoside hydrolases. Previous studies have elucidated the structures of several fungal and two bacterial galactanases, while biochemical studies have indicated differences in the product profiles of different members of the family. Structural studies of ligand complexes have to date been limited to the bacterial members of the family. Here, the first structure of a fungal galactanase in complex with a disaccharide is presented. Galactobiose binds to subsites -1 and -2, thus improving our understanding of ligand binding to galactanases.The structure of Aspergillus aculeatus β-1,4-galactanase, a glycoside hydrolase belonging to family 53, has been determined in complex with galactobiose at subsites -1 and -2.

Originalsprog	Engelsk
Tidsskrift	Acta Crystallographica Section F: Structural Biology Communications
Vol/bind	75
Udgave nummer	6
Sider (fra-til)	399-404
Antal sider	6
ISSN	2053-230X
DOI	https://doi.org/10.1107/S2053230X19005612
Status	Udgivet - jun. 2019

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10.1107/S2053230X19005612

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Citationsformater

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title = "Structure of Aspergillus aculeatus β-1,4-galactanase in complex with galactobiose",

abstract = "β-1,4-Galactanases are glycoside hydrolases that are involved in the degradation of pectin and belong to family 53 in the classification of glycoside hydrolases. Previous studies have elucidated the structures of several fungal and two bacterial galactanases, while biochemical studies have indicated differences in the product profiles of different members of the family. Structural studies of ligand complexes have to date been limited to the bacterial members of the family. Here, the first structure of a fungal galactanase in complex with a disaccharide is presented. Galactobiose binds to subsites -1 and -2, thus improving our understanding of ligand binding to galactanases.The structure of Aspergillus aculeatus β-1,4-galactanase, a glycoside hydrolase belonging to family 53, has been determined in complex with galactobiose at subsites -1 and -2.",

author = "S{\o}s Torpenholt and Poulsen, {Jens-christian N.} and Muderspach, {Sebastian Jannick} and {De Maria}, Leonardo and {Lo Leggio}, Leila",

year = "2019",

month = jun,

doi = "10.1107/S2053230X19005612",

language = "English",

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pages = "399--404",

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T1 - Structure of Aspergillus aculeatus β-1,4-galactanase in complex with galactobiose

AU - Torpenholt, Søs

AU - Poulsen, Jens-christian N.

AU - Muderspach, Sebastian Jannick

AU - De Maria, Leonardo

AU - Lo Leggio, Leila

PY - 2019/6

Y1 - 2019/6

N2 - β-1,4-Galactanases are glycoside hydrolases that are involved in the degradation of pectin and belong to family 53 in the classification of glycoside hydrolases. Previous studies have elucidated the structures of several fungal and two bacterial galactanases, while biochemical studies have indicated differences in the product profiles of different members of the family. Structural studies of ligand complexes have to date been limited to the bacterial members of the family. Here, the first structure of a fungal galactanase in complex with a disaccharide is presented. Galactobiose binds to subsites -1 and -2, thus improving our understanding of ligand binding to galactanases.The structure of Aspergillus aculeatus β-1,4-galactanase, a glycoside hydrolase belonging to family 53, has been determined in complex with galactobiose at subsites -1 and -2.

AB - β-1,4-Galactanases are glycoside hydrolases that are involved in the degradation of pectin and belong to family 53 in the classification of glycoside hydrolases. Previous studies have elucidated the structures of several fungal and two bacterial galactanases, while biochemical studies have indicated differences in the product profiles of different members of the family. Structural studies of ligand complexes have to date been limited to the bacterial members of the family. Here, the first structure of a fungal galactanase in complex with a disaccharide is presented. Galactobiose binds to subsites -1 and -2, thus improving our understanding of ligand binding to galactanases.The structure of Aspergillus aculeatus β-1,4-galactanase, a glycoside hydrolase belonging to family 53, has been determined in complex with galactobiose at subsites -1 and -2.

U2 - 10.1107/S2053230X19005612

DO - 10.1107/S2053230X19005612

M3 - Journal article

C2 - 31204685

SN - 2053-230X

VL - 75

SP - 399

EP - 404

JO - Acta Crystallographica Section F: Structural Biology Communications

JF - Acta Crystallographica Section F: Structural Biology Communications

IS - 6

ER -

Structure of Aspergillus aculeatus β-1,4-galactanase in complex with galactobiose

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