The C-terminus of dUTPase: observation on flexibility using NMR.
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.
Department of Biochemistry, Center for Chemistry and Chemical Engineering, Lund University, Sweden. johan.nord@astrazeneca
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J
Nord
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P
Nyman
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G
Larsson
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Drakenberg
D004926:Escherichia coli / Q000201:enzymology*; D004860:Infectious Anemia Virus, Equine / Q000201:enzymology*; D009682:Magnetic Resonance Spectroscopy; D009711:Nucleotides / Q000737:chemistry; D018583:Pliability; D011487:Protein Conformation; D011755:Pyrophosphatases / Q000737:chemistry* / Q000378:metabolism
D009711:Nucleotides; D011755:Pyrophosphatases; C020020:dUTP pyrophosphatase