Structural analysis of the inactive state of the Escherichia coli DNA polymerase clamp-loader complex

Kazmirski et al. 10.1073/pnas.0407904101.

Supporting Information

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Supporting Figure 5
Supporting Figure 6
Supporting Figure 7




Fig. 5. Surface representations of the nucleotide-free and nucleotide-bound crystal structures of the clamp-loader complex. In black are residues that are involved in crystal contacts in the lattice. Each of the crystal structures has a unique pattern of crystal contacts.





Fig. 6. Superposition of domain I of g C from the nucleotide-free and ATPg S-bound crystal structures. g C is shown in red. g D for the ATPg S-bound clamp loader (green) shows very little change in position with respect to gD of the nucleotide-free clamp loader (gray), which suggests that binding of ATP alone is not responsible for opening the ATP binding site on gC, and other factors such as the bclamp may be necessary to cause the conformational change.





Fig. 7. Root-mean-square deviation in Ca positions with respect to the crystal structure for each of the domains of the clamp loader crystal structure: domain I (A), domain II (B), and domain III (C). For domain I the N-terminal 20 residues and the zinc-finger have been removed. From domain III, the C-terminal five residues have been removed. The colors for the subunits are magenta (d A), blue (g B), red (g C), green (g D), and orange (d 'E).

This Article

  1. Published online before print November 19, 2004, doi: 10.1073/pnas.0407904101 PNAS November 30, 2004 vol. 101 no. 48 16750-16755
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