PMID:11257499
| Citation |
Nord, J, Nyman, P, Larsson, G and Drakenberg, T (2001) The C-terminus of dUTPase: observation on flexibility using NMR. FEBS Lett. 492:228-32 |
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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-(15)N 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. |
| Links | |
| Keywords |
Escherichia coli/enzymology; Infectious Anemia Virus, Equine/enzymology; Magnetic Resonance Spectroscopy; Nucleotides/chemistry; Pliability; Protein Conformation; Pyrophosphatases/chemistry; Pyrophosphatases/metabolism |
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