The C-terminus of dUTPase: observation on flexibility using NMR

Johan Nord; Per-Olof Nyman; Gunilla Larsson; Torbjörn Drakenberg

doi:10.1016/S0014-5793(01)02257-8

The C-terminus of dUTPase: observation on flexibility using NMR

Johan Nord, Per-Olof Nyman, Gunilla Larsson, Torbjörn Drakenberg

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

Abstract

The dynamics of the C-terminus of the dUTPases from Escherichia coli and equine infectious anaemia virus (EIAV) were studied by 1H-15N nuclear magnetic resonance spectroscopy. The two enzymes differ with regard to flexibility in the backbone of the 15 most C-terminal amino acid residues, some of which are conserved and essential for enzymic activity. In the bacterial enzyme, the residues closest to the C-terminus are highly flexible and display a correlation time in the nanosecond time range. No similar high flexibility could be detected for the C-terminal part of EIAV dUTPase, indicating a different time range of flexibility.

Original language	English
Pages (from-to)	228-232
Journal	FEBS Letters
Volume	492
Issue number	3
DOIs	https://doi.org/10.1016/S0014-5793(01)02257-8
Publication status	Published - 2001

Subject classification (UKÄ)

Biological Sciences

Free keywords

dUTPase
Equine infectious anemia virus
Flexible C-terminus
Nuclear magnetic resonance
Nucleotide binding
Escherichia coli

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10.1016/S0014-5793(01)02257-8

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title = "The C-terminus of dUTPase: observation on flexibility using NMR",

abstract = "The dynamics of the C-terminus of the dUTPases from Escherichia coli and equine infectious anaemia virus (EIAV) were studied by 1H-15N nuclear magnetic resonance spectroscopy. The two enzymes differ with regard to flexibility in the backbone of the 15 most C-terminal amino acid residues, some of which are conserved and essential for enzymic activity. In the bacterial enzyme, the residues closest to the C-terminus are highly flexible and display a correlation time in the nanosecond time range. No similar high flexibility could be detected for the C-terminal part of EIAV dUTPase, indicating a different time range of flexibility.",

keywords = "dUTPase, Equine infectious anemia virus, Flexible C-terminus, Nuclear magnetic resonance, Nucleotide binding, Escherichia coli",

author = "Johan Nord and Per-Olof Nyman and Gunilla Larsson and Torbj{\"o}rn Drakenberg",

year = "2001",

doi = "10.1016/S0014-5793(01)02257-8",

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volume = "492",

pages = "228--232",

journal = "FEBS Letters",

issn = "1873-3468",

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T1 - The C-terminus of dUTPase: observation on flexibility using NMR

AU - Nord, Johan

AU - Nyman, Per-Olof

AU - Larsson, Gunilla

AU - Drakenberg, Torbjörn

PY - 2001

Y1 - 2001

N2 - The dynamics of the C-terminus of the dUTPases from Escherichia coli and equine infectious anaemia virus (EIAV) were studied by 1H-15N nuclear magnetic resonance spectroscopy. The two enzymes differ with regard to flexibility in the backbone of the 15 most C-terminal amino acid residues, some of which are conserved and essential for enzymic activity. In the bacterial enzyme, the residues closest to the C-terminus are highly flexible and display a correlation time in the nanosecond time range. No similar high flexibility could be detected for the C-terminal part of EIAV dUTPase, indicating a different time range of flexibility.

AB - The dynamics of the C-terminus of the dUTPases from Escherichia coli and equine infectious anaemia virus (EIAV) were studied by 1H-15N nuclear magnetic resonance spectroscopy. The two enzymes differ with regard to flexibility in the backbone of the 15 most C-terminal amino acid residues, some of which are conserved and essential for enzymic activity. In the bacterial enzyme, the residues closest to the C-terminus are highly flexible and display a correlation time in the nanosecond time range. No similar high flexibility could be detected for the C-terminal part of EIAV dUTPase, indicating a different time range of flexibility.

KW - dUTPase

KW - Equine infectious anemia virus

KW - Flexible C-terminus

KW - Nuclear magnetic resonance

KW - Nucleotide binding

KW - Escherichia coli

UR - https://www.scopus.com/pages/publications/0035896405

U2 - 10.1016/S0014-5793(01)02257-8

DO - 10.1016/S0014-5793(01)02257-8

M3 - Article

SN - 1873-3468

VL - 492

SP - 228

EP - 232

JO - FEBS Letters

JF - FEBS Letters

IS - 3

ER -

The C-terminus of dUTPase: observation on flexibility using NMR

Abstract

Subject classification (UKÄ)

Free keywords

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