Unliganded and substrate bound structures of the cellooligosaccharide active lytic polysaccharide monooxygenase LsAA9A at low pH

Kristian Erik Høpfner Frandsen; Jens-Christian Navarro Poulsen; Tobias Tandrup; Leila Lo Leggio

doi:10.1016/j.carres.2017.03.010

Unliganded and substrate bound structures of the cellooligosaccharide active lytic polysaccharide monooxygenase LsAA9A at low pH

Kristian Erik Høpfner Frandsen, Jens-Christian Navarro Poulsen, Tobias Tandrup, Leila Lo Leggio^*

^*Corresponding author for this work

Department of Chemistry

15 Citations (Scopus)

Abstract

Lytic polysaccharide monooxygenases (LPMOs) have been found to be key components in microbial (bacterial and fungal) degradation of biomass. They are copper metalloenzymes that degrade polysaccharides oxidatively and act in synergy with glycoside hydrolases. Recently crystallographic studies carried out at pH 5.5 of the LPMO from Lentinus similis belonging to the fungal LPMO family AA9 have provided the first atomic resolution view of substrate-LPMO interactions. The LsAA9A structure presented here determined at pH 3.5 shows significant disorder of the active site in the absence of substrate ligand. Furthermore some differences are also observed in regards to substrate (cellohexaose) binding, although the major interaction with the N-terminal histidine remains unchanged.

Original language	English
Journal	Carbohydrate Research
Volume	448
Pages (from-to)	187-190
Number of pages	4
ISSN	0008-6215
DOIs	https://doi.org/10.1016/j.carres.2017.03.010
Publication status	Published - 2017

Keywords

Cellohexaose interactions
Lytic polysaccharide monooxygenases
PH-dependent disorder

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10.1016/j.carres.2017.03.010

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title = "Unliganded and substrate bound structures of the cellooligosaccharide active lytic polysaccharide monooxygenase LsAA9A at low pH",

abstract = "Lytic polysaccharide monooxygenases (LPMOs) have been found to be key components in microbial (bacterial and fungal) degradation of biomass. They are copper metalloenzymes that degrade polysaccharides oxidatively and act in synergy with glycoside hydrolases. Recently crystallographic studies carried out at pH 5.5 of the LPMO from Lentinus similis belonging to the fungal LPMO family AA9 have provided the first atomic resolution view of substrate-LPMO interactions. The LsAA9A structure presented here determined at pH 3.5 shows significant disorder of the active site in the absence of substrate ligand. Furthermore some differences are also observed in regards to substrate (cellohexaose) binding, although the major interaction with the N-terminal histidine remains unchanged.",

keywords = "Cellohexaose interactions, Lytic polysaccharide monooxygenases, PH-dependent disorder",

author = "Frandsen, {Kristian Erik H{\o}pfner} and Poulsen, {Jens-Christian Navarro} and Tobias Tandrup and {Lo Leggio}, Leila",

year = "2017",

doi = "10.1016/j.carres.2017.03.010",

language = "English",

volume = "448",

pages = "187--190",

journal = "Carbohydrate Research",

issn = "0008-6215",

publisher = "Pergamon Press",

}

TY - JOUR

T1 - Unliganded and substrate bound structures of the cellooligosaccharide active lytic polysaccharide monooxygenase LsAA9A at low pH

AU - Frandsen, Kristian Erik Høpfner

AU - Poulsen, Jens-Christian Navarro

AU - Tandrup, Tobias

AU - Lo Leggio, Leila

PY - 2017

Y1 - 2017

N2 - Lytic polysaccharide monooxygenases (LPMOs) have been found to be key components in microbial (bacterial and fungal) degradation of biomass. They are copper metalloenzymes that degrade polysaccharides oxidatively and act in synergy with glycoside hydrolases. Recently crystallographic studies carried out at pH 5.5 of the LPMO from Lentinus similis belonging to the fungal LPMO family AA9 have provided the first atomic resolution view of substrate-LPMO interactions. The LsAA9A structure presented here determined at pH 3.5 shows significant disorder of the active site in the absence of substrate ligand. Furthermore some differences are also observed in regards to substrate (cellohexaose) binding, although the major interaction with the N-terminal histidine remains unchanged.

AB - Lytic polysaccharide monooxygenases (LPMOs) have been found to be key components in microbial (bacterial and fungal) degradation of biomass. They are copper metalloenzymes that degrade polysaccharides oxidatively and act in synergy with glycoside hydrolases. Recently crystallographic studies carried out at pH 5.5 of the LPMO from Lentinus similis belonging to the fungal LPMO family AA9 have provided the first atomic resolution view of substrate-LPMO interactions. The LsAA9A structure presented here determined at pH 3.5 shows significant disorder of the active site in the absence of substrate ligand. Furthermore some differences are also observed in regards to substrate (cellohexaose) binding, although the major interaction with the N-terminal histidine remains unchanged.

KW - Cellohexaose interactions

KW - Lytic polysaccharide monooxygenases

KW - PH-dependent disorder

U2 - 10.1016/j.carres.2017.03.010

DO - 10.1016/j.carres.2017.03.010

M3 - Journal article

C2 - 28364950

AN - SCOPUS:85016489386

SN - 0008-6215

VL - 448

SP - 187

EP - 190

JO - Carbohydrate Research

JF - Carbohydrate Research

ER -

Unliganded and substrate bound structures of the cellooligosaccharide active lytic polysaccharide monooxygenase LsAA9A at low pH

Abstract

Keywords

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