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. Author manuscript; available in PMC: 2013 Feb 1.
Published in final edited form as: Mol Microbiol. 2012 Jan 10;83(3):457–470. doi: 10.1111/j.1365-2958.2011.07919.x

Fig. 1. Ribbon diagram of AphB.

Fig. 1

(A) The asymmetric unit of the full-length AphB structure contains one extended subunit (grey) and one compact subunit (color) that dimerize through their linker helices to form a coiled-coil. In the compact subunit, the DNA-binding domain (DBD, cyan) and linker helix (green) are folded in toward the regulatory domain (RD, magenta), whereas in the extended subunit, the DNA-binding domain and linker helix point away from the RD. (B) The DNA binding domain (residues 1-58) of AphB consists of a winged helix-turn-helix motif. (C) The regulatory domain of AphB contains two subdomains: RD-1 (residues 90-159 and residues 262-291) and RD-II (residues 160-261) colored from N-terminal residue (S90, blue) to the C-terminus (red). All figures were created using MacPyMOL (DeLano, 2002).