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Figure 5
Charge distribution and DNA binding. (a) Surface-charge distribution for the TrxT (left) and Dhd (right) proteins. Both sides of the surface are displayed. The catalytic site, the α3 helix and the C-terminal CIVD motif of TrxT are indicated. (b) Surface-charge distribution of Dhd proteins generated using the Dm Dhd structure as a template. The molecules are oriented as in the top view in (a). The other side is represented in Supplementary Fig. S4(c). (c) The DNA-binding capacity of Dm Dhd compared with those of lysozyme, BSA and the MH1 domain of Smad3. Protein concentrations are indicated at the top of the gel. The DNA is at 7.5 nM. Dm Dhd and Smad3 interact with DNA at a 40 equivalents protein excess, although the interaction of Dhd is nonspecific whereas Smad3 binds to a single site in this DNA.

IUCrJ
Volume 8| Part 2| March 2021| Pages 281-294
ISSN: 2052-2525