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. 2008 Aug 20;105(34):12194–12199. doi: 10.1073/pnas.0803154105

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© 2008 by The National Academy of Sciences of the USA

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Fig. 5. — Structural homology and interface residue conservation displayed by the C. perfringens X82 modules. (A) Backbone overlay (N, C_α, C′ atoms) of CpGH84CX82 (green) from the CpGH84CX82-μ-toxin FIVAR-Doc complex structure and isolated NanJX82 (salmon). (B) Overlay of the 9a-8-3-6-5 X82 faces and from CpGH84CX82 (green) and NanJX82 (salmon) depicting the Doc recognition residues of CpGH84CX82 and the analogous residues in NanJX82 as stick models. Residues are identified by one-letter code, and colored and numbered accordingly.