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

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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.

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Subject classification (UKÄ) – MANDATORY

  • Biological Sciences

Keywords

  • dUTPase, Equine infectious anemia virus, Flexible C-terminus, Nuclear magnetic resonance, Nucleotide binding, Escherichia coli
Original languageEnglish
Pages (from-to)228-232
JournalFEBS Letters
Volume492
Issue number3
Publication statusPublished - 2001
Publication categoryResearch
Peer-reviewedYes