1H, 13C and 15N backbone and side-chain assignment of a carbohydrate binding module from a xylanase from Roseburia intestinalis

Eva Madland; Yoshihito Kitaoku; Gerd Inger Sætrom; Maria Louise Leth; Morten Ejby; Maher Abou Hachem; Finn Lillelund Aachmann

doi:10.1007/s12104-018-9850-3

1H, 13C and 15N backbone and side-chain assignment of a carbohydrate binding module from a xylanase from Roseburia intestinalis

Eva Madland, Yoshihito Kitaoku, Gerd Inger Sætrom, Maria Louise Leth, Morten Ejby, Maher Abou Hachem, Finn Lillelund Aachmann

Research output: Contribution to journal › Article › peer-review

2 Citations (Scopus)

Abstract

The N-terminal domain (residues 28-165) from the glycoside hydrolase family 10 from Roseburia intestinalis (RiCBMx), has been isotopically labeled and recombinantly expressed in Escherichia coli. Here we report 1H, 13C and 15N NMR chemical shift assignments for this carbohydrate binding module (CBM).

Original language	English
Pages (from-to)	55-58
Number of pages	4
Journal	Biomolecular NMR Assignments
Volume	13
Issue number	1
DOIs	https://doi.org/10.1007/s12104-018-9850-3
Publication status	Published - Apr 2019
Externally published	Yes

Keywords

Carbon Isotopes
Endo-1,4-beta Xylanases/chemistry
Firmicutes/enzymology
Nitrogen Isotopes
Nuclear Magnetic Resonance, Biomolecular
Protein Structure, Secondary
Protons
Receptors, Cell Surface/chemistry

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10.1007/s12104-018-9850-3

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title = "1H, 13C and 15N backbone and side-chain assignment of a carbohydrate binding module from a xylanase from Roseburia intestinalis",

abstract = "The N-terminal domain (residues 28-165) from the glycoside hydrolase family 10 from Roseburia intestinalis (RiCBMx), has been isotopically labeled and recombinantly expressed in Escherichia coli. Here we report 1H, 13C and 15N NMR chemical shift assignments for this carbohydrate binding module (CBM).",

keywords = "Carbon Isotopes, Endo-1,4-beta Xylanases/chemistry, Firmicutes/enzymology, Nitrogen Isotopes, Nuclear Magnetic Resonance, Biomolecular, Protein Structure, Secondary, Protons, Receptors, Cell Surface/chemistry",

author = "Eva Madland and Yoshihito Kitaoku and S{\ae}trom, {Gerd Inger} and Leth, {Maria Louise} and Morten Ejby and Hachem, {Maher Abou} and Aachmann, {Finn Lillelund}",

year = "2019",

month = apr,

doi = "10.1007/s12104-018-9850-3",

language = "English",

volume = "13",

pages = "55--58",

journal = "Biomolecular NMR Assignments",

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publisher = "Springer Netherlands",

number = "1",

}

TY - JOUR

T1 - 1H, 13C and 15N backbone and side-chain assignment of a carbohydrate binding module from a xylanase from Roseburia intestinalis

AU - Madland, Eva

AU - Kitaoku, Yoshihito

AU - Sætrom, Gerd Inger

AU - Leth, Maria Louise

AU - Ejby, Morten

AU - Hachem, Maher Abou

AU - Aachmann, Finn Lillelund

PY - 2019/4

Y1 - 2019/4

N2 - The N-terminal domain (residues 28-165) from the glycoside hydrolase family 10 from Roseburia intestinalis (RiCBMx), has been isotopically labeled and recombinantly expressed in Escherichia coli. Here we report 1H, 13C and 15N NMR chemical shift assignments for this carbohydrate binding module (CBM).

AB - The N-terminal domain (residues 28-165) from the glycoside hydrolase family 10 from Roseburia intestinalis (RiCBMx), has been isotopically labeled and recombinantly expressed in Escherichia coli. Here we report 1H, 13C and 15N NMR chemical shift assignments for this carbohydrate binding module (CBM).

KW - Carbon Isotopes

KW - Endo-1,4-beta Xylanases/chemistry

KW - Firmicutes/enzymology

KW - Nitrogen Isotopes

KW - Nuclear Magnetic Resonance, Biomolecular

KW - Protein Structure, Secondary

KW - Protons

KW - Receptors, Cell Surface/chemistry

U2 - 10.1007/s12104-018-9850-3

DO - 10.1007/s12104-018-9850-3

M3 - Article

C2 - 30244308

VL - 13

SP - 55

EP - 58

JO - Biomolecular NMR Assignments

JF - Biomolecular NMR Assignments

SN - 1874-2718

IS - 1

ER -

1H, 13C and 15N backbone and side-chain assignment of a carbohydrate binding module from a xylanase from Roseburia intestinalis

Abstract

Keywords

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