The dynamics of the C-terminus of the dUTPases from Escherichia coli and eq
uine infectious anaemia virus (EIAV) were studied by H-1-N-15 nuclear magne
tic resonance spectroscopy. The two enzymes differ with regard to flexibili
ty in the backbone of the 15 most C-terminal amino acid residues, some of w
hich are conserved and essential for enzymic activity. In the bacterial enz
yme, the residues closest to the C-terminus are highly flexible and display
a correlation time in the nanosecond time range. No similar high flexibili
ty could be detected for the C-terminal part of EIAV dUTPase, indicating a
different time range of flexibility. (C) 2001 Federation of European Bioche
mical Societies. Published by Elsevier Science B.V. All rights reserved.