Figure 4.
Fig. 4. Structure of EI-N119S in complex with RB-AZT-TP.
A, the x-ray structure of the triple mutant of Dictyostelium NDP
kinase (yellow bonds) in complex with the R[p] stereoisomer of
the -borano
analog of AZT triphosphate is compared with that of the wild
type protein in complex with TDP (21) (blue bonds). The
orientation is as in Fig. 1, and the mutated side chains at
positions 64, 119, and 122 are in ball-and-stick representation.
B, the same structure (yellow bonds) is compared with that of
the complex with AZT diphosphate (Ref. 20, purple bonds).
Movements of the sugar ring, of the azido group (N3), and of the
Lys-16 side chain may explain the improved efficiency of the
enzyme bearing the N119S mutation. Despite these changes and of
the -borano
(BH3) substitution, the - and -phosphates
superimpose exactly.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2002,
277,
39953-39959)
copyright 2002.
-borano
analog of AZT triphosphate is compared with that of the wild
type protein in complex with TDP (21) (blue bonds). The
orientation is as in Fig. 1, and the mutated side chains at
positions 64, 119, and 122 are in ball-and-stick representation.
B, the same structure (yellow bonds) is compared with that of
the complex with AZT diphosphate (Ref. 20, purple bonds).
Movements of the sugar ring, of the azido group (N3), and of the
Lys-16 side chain may explain the improved efficiency of the
enzyme bearing the N119S mutation. Despite these changes and of
the 
-phosphates
superimpose exactly.