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Figure 2 | BMC Molecular Biology

Figure 2

From: A single hydrophobic cleft in the Escherichia coli processivity clamp is sufficient to support cell viability and DNA damage-induced mutagenesis in vivo

Figure 2

Sliding clamp mutations utilized in this study. (A) Positions of mutations present in β159 (G66E and G174A) are represented as yellow space filled atoms on the structure of the wild-type clamp. (B) Proposed structure of the βC/β159 heterodimer. Positions of G66E and G174A substitutions in β159 are represented as yellow space filled atoms, while residues 362-366, which are deleted from βC, are colored red. (C) Structure of the Pol IV little finger (Pol IVLF) domain in complex with the β clamp as reported by Bunting et al. [14]. Pol IVLF is in purple. Pol IVLF contacts residues E93 and L98, as well as 362-366 of the clamp; position of E93K and L98K substitutions (yellow), and Δ362-366 (red) are indicated. (D) Positions of the E93K-L98K and I272A-L273A mutations used to characterize the ability of βC to complement the temperature sensitive growth phenotype of the dnaN159 strain are shown on the presumed structure of the βC/β159 heterodimer, which bears the G66E, G174A, and Δ362-366 mutations. Figures were generated using Imol, and the coordinates for either the wild-type clamp (2POL), or the β clamp-Pol IV little finger complex (1UNN) obtained from the PDB.

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