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The EMBO Journal (2003) 22, 4910–4921, doi:10.1093/emboj/cdg500

Figure 6
High-resolution structure of the E.coli RecQ helicase catalytic core
Douglas A. Bernstein, Morgan C. Zittel and James L. Keck
Figure 6
Figure 6
Models for DNA binding to E.coli RecQDeltaC. Surface representations of E.coli RecQDeltaC are shown (color-coded as in Figure 1, inset left) bound to cartoon diagrams of a partially unwound DNA molecule in two possible orientations (yellow). The RecQDeltaC surface is colored by its electrostatic surface potential (inset right and main panel) at + or -6 kBT/e for positive (blue) or negative (red) charge potential using the program GRASP (Nicholls et al., 1991). Since E.coli RecQ may unwind DNA as an oligomer (Harmon and Kowalczykowski, 2001), it is not clear whether ssDNA bound by the helicase region would come from dsDNA bound by the same protomer or another protomer in the oligomer during unwinding. As such, the connection linking the dsDNA to the 3' ssDNA is shown as a dashed line. In addition, relative subdomain orientations could change in the DNA-bound form.
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