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

Summary, in English

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.

• Författare: Johan Nord; Per-Olof Nyman; Gunilla Larsson; Torbjörn Drakenberg
• Avdelning/ar: Biokemi och Strukturbiologi; Kemiska institutionen
• Publiceringsår: 2001
• Språk: Engelska
• Sidor: 228-232
• Publikation/Tidskrift/Serie: FEBS Letters
• Volym: 492
• Issue: 3
• Länkar: http://dx.doi.org/10.1016/S0014-5793(01)02257-8
• Dokumenttyp: Artikel i tidskrift
• Förlag: Wiley-Blackwell
• Ämne: Biological Sciences
• Nyckelord: dUTPase; Equine infectious anemia virus; Flexible C-terminus; Nuclear magnetic resonance; Nucleotide binding; Escherichia coli
• Status: Published
• ISBN/ISSN/Övrigt: ISSN: 1873-3468