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. Author manuscript; available in PMC: 2011 Feb 7.
Published in final edited form as: J Mol Biol. 2004 Feb 13;336(2):381–393. doi: 10.1016/j.jmb.2003.12.043

Figure 8.

Figure 8

The architecture of the τ–DnaB complex. (A) The shape of the B. subtilis τ protein resembles the E. coli clamp–loader complex. Comparison of the AFM topography image of τ (top) with the crystal structure of the clamp– loader complex (middle). (B) The architecture of the complex based upon the AFM topography image shown (top). Two possible orientations of the clamp-loader complex are shown. Arrows indicate the C-termini of the black and blue subunits (equivalent to τ1 and τ2, respectively) and the L73, F74 residues of δ that interact with the β clamp. (C) A model of the τ-DnaB complex. The clamp-loader interacts with the helicase via two Cτ domains of two τ subunits.