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 |
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Pages (from-to) | 228-232 |
Journal | FEBS Letters |
Volume | 492 |
Issue number | 3 |
DOIs | |
Publication status | Published - 2001 |
Subject classification (UKÄ)
- Biological Sciences
Keywords
- dUTPase
- Equine infectious anemia virus
- Flexible C-terminus
- Nuclear magnetic resonance
- Nucleotide binding
- Escherichia coli