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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. 2. Ribbon diagram of the AphB tetramer.

Fig. 2

(A) The AphB tetramer is composed of four subunits, two in the extended (yellow, cyan) conformation and two in the compact (magenta, green) conformation. The N-terminal dimerization interface (left inset), along the linker helices of subunit A and B, is composed of polar, charged and hydrophobic residues. The head-to-tail interaction of the regulatory domain of subunit A with the regulatory domain of subunit D forms the second dimerization interface (right inset). (B) Schematic showing the overall fold of AphB, which is formed by four subunits, each composed of a regulatory domain (rectangles) connected to a DNA-binding domain (triangles) via a linker helix (cylinders).