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

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Standard

Unliganded and substrate bound structures of the cellooligosaccharide active lytic polysaccharide monooxygenase LsAA9A at low pH. / Frandsen, Kristian Erik Høpfner; Poulsen, Jens-Christian Navarro; Tandrup, Tobias; Lo Leggio, Leila.

I: Carbohydrate Research, Bind 448, 2017, s. 187-190.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Frandsen, KEH, Poulsen, J-CN, Tandrup, T & Lo Leggio, L 2017, 'Unliganded and substrate bound structures of the cellooligosaccharide active lytic polysaccharide monooxygenase LsAA9A at low pH', Carbohydrate Research, bind 448, s. 187-190. https://doi.org/10.1016/j.carres.2017.03.010

APA

Frandsen, K. E. H., Poulsen, J-C. N., Tandrup, T., & Lo Leggio, L. (2017). Unliganded and substrate bound structures of the cellooligosaccharide active lytic polysaccharide monooxygenase LsAA9A at low pH. Carbohydrate Research, 448, 187-190. https://doi.org/10.1016/j.carres.2017.03.010

Vancouver

Frandsen KEH, Poulsen J-CN, Tandrup T, Lo Leggio L. Unliganded and substrate bound structures of the cellooligosaccharide active lytic polysaccharide monooxygenase LsAA9A at low pH. Carbohydrate Research. 2017;448:187-190. https://doi.org/10.1016/j.carres.2017.03.010

Author

Frandsen, Kristian Erik Høpfner ; Poulsen, Jens-Christian Navarro ; Tandrup, Tobias ; Lo Leggio, Leila. / Unliganded and substrate bound structures of the cellooligosaccharide active lytic polysaccharide monooxygenase LsAA9A at low pH. I: Carbohydrate Research. 2017 ; Bind 448. s. 187-190.

Bibtex

@article{cdc51c893778480faa2ffc7ad1ddaa93,
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",

}

RIS

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

VL - 448

SP - 187

EP - 190

JO - Carbohydrate Research

JF - Carbohydrate Research

SN - 0008-6215

ER -

ID: 176611787