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. Author manuscript; available in PMC: 2015 Dec 7.
Published in final edited form as: Biochem J. 2011 Jul 15;437(2):243–253. doi: 10.1042/BJ20110304

Figure 4. Crystal structure of DUT1.

Figure 4

(A) DUT1 monomer. (B) Ribbon diagram showing the DUT1 trimer (top view) with three molecules of α,β-imido dUTP (shown as spheres) bound to the active sites located between the subunits. DUT1 subunits are shown in different colours. (C and D) Surface presentation of the DUT1 active site with the bound α,β-imido dUTP (C) or dUMP (D) (shown as sticks). The protein subunits are shown in different colours (pink, light green and light grey), and in (D) the surface has been rendered semi-transparent to show the bound nucleotide. Note that in (D) dUMP is almost completely covered by the C-terminal tail (grey), which is disordered in (C) and the active site with bound α,β-imido dUTP is open.